{"gene":"FABP7","run_date":"2026-04-28T17:46:03","timeline":{"discoveries":[{"year":1994,"finding":"BLBP (FABP7) is a brain-specific lipid-binding protein expressed in radial glia that localizes to both nucleus and cytoplasm, and is required for establishment of the radial glial fiber system in developing brain; antibody-mediated blockade of BLBP disrupts glial and neuronal differentiation in primary cell cultures without affecting proliferation or adhesion.","method":"Immunoelectron microscopy (subcellular localization), anti-BLBP antibody blockade in primary cell cultures (functional loss-of-function), in situ hybridization and immunocytochemistry (expression pattern)","journal":"Neuron","confidence":"High","confidence_rationale":"Tier 2 — direct protein localization by immunoelectron microscopy plus functional antibody-blockade assay with defined phenotypic readout; foundational paper with 488 citations","pmids":["8161459"],"is_preprint":false},{"year":2005,"finding":"Fabp7 is a downstream transcriptional target of Pax6 in the developing rat cortex; Fabp7 siRNA knockdown curtails neuroepithelial cell proliferation and promotes premature neuronal differentiation, demonstrating Fabp7 is required for maintenance of neuroepithelial cells.","method":"Microarray followed by quantitative PCR (expression), electroporation of siRNA in embryonic rat cortex (in vivo loss-of-function), Pax6 overexpression (gain-of-function), BrdU proliferation assay","journal":"The Journal of neuroscience","confidence":"High","confidence_rationale":"Tier 2 — in vivo siRNA knockdown with specific proliferation/differentiation phenotype plus epistasis (Pax6 overexpression inducing Fabp7); replicated observations in multiple model conditions","pmids":["16237179"],"is_preprint":false},{"year":2007,"finding":"Fabp7-deficient mice show decreased prepulse inhibition and disrupted neurogenesis in vivo, placing Fabp7 in a pathway linking NMDA receptor signaling, glial function, and sensorimotor gating; genetic complementation test supported Fabp7 as the QTL gene.","method":"QTL analysis, Fabp7 knockout mice behavioral phenotyping (PPI assay), BrdU neurogenesis assay, quantitative complementation test","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal methods (QTL mapping, KO phenotyping, quantitative complementation, neurogenesis assay) in a single highly-cited study","pmids":["18001149"],"is_preprint":false},{"year":2003,"finding":"PKNOX1 (PREP1), a transcription factor encoded on chromosome 21, directly binds the Pbx/POU site of the FABP7 promoter in vitro and transactivates FABP7 promoter activity in neuroblastoma cells, linking chromosome 21 gene-dosage imbalance in Down syndrome to FABP7 overexpression.","method":"Genomic inverse PCR (promoter cloning), in vitro binding assay (PKNOX1 binding to FABP7 promoter), transfection/promoter transactivation assay in neuroblastoma cells, real-time PCR","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 2 — in vitro binding and promoter transactivation assays with functional context; single lab","pmids":["12771203"],"is_preprint":false},{"year":2008,"finding":"Brain fatty acid-binding protein Fabp7 mRNA and protein levels undergo diurnal oscillations throughout adult mouse brain, with mRNA peaking during the light period and protein peaking during the dark period; this diurnal rhythm is present in astrocytes and hippocampal granule cell precursors but is absent in immature postnatal brain where astrocytes are not yet mature.","method":"RNA analysis, in situ hybridization, immunoblot (diurnal expression profiling across 24 h in adult and postnatal mouse brain)","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 — direct measurement of mRNA and protein at multiple time points across brain regions; single lab but comprehensive","pmids":["18286188"],"is_preprint":false},{"year":2011,"finding":"FABP7 is required for astrocyte proliferation following brain stab injury; FABP7-KO astrocytes show decreased proliferation and reduced omega-3 fatty acid incorporation, linking FABP7 to cellular fatty acid homeostasis in reactive gliosis.","method":"Mouse cortical stab injury model, Western blot, immunohistochemistry, BrdU proliferation assay in FABP7-KO vs wild-type mice, primary astrocyte culture from KO mice","journal":"Histochemistry and cell biology","confidence":"High","confidence_rationale":"Tier 2 — in vivo KO model with defined proliferation phenotype plus in vitro primary astrocyte validation; multiple orthogonal methods","pmids":["21938553"],"is_preprint":false},{"year":2012,"finding":"Fabp7 and Fabp5 are differentially expressed in postnatal hippocampal neural stem/progenitor cells; Fabp7 KO reduces NSC/NPC proliferation and BrdU uptake while enhancing neuronal differentiation in the subgranular zone of the dentate gyrus.","method":"Immunofluorescence, BrdU pulse-chase assay, Fabp7 KO / Fabp5 KO / double-KO mouse analysis","journal":"Stem cells (Dayton, Ohio)","confidence":"High","confidence_rationale":"Tier 2 — multiple KO genotypes with BrdU proliferation and survival assays; replicated across anterior-posterior axis","pmids":["22581784"],"is_preprint":false},{"year":2012,"finding":"FABP7 mRNA localizes to the astrocytic perisynaptic compartment and undergoes diurnal changes in intracellular distribution; Fabp7 mRNA co-immunoprecipitates with CPEB1 from primary astrocyte extracts, and its 3'UTR contains functional cytoplasmic polyadenylation elements (CPEs) capable of regulating mRNA translation, implicating circadian/sleep-dependent polyadenylation in subcellular trafficking of Fabp7 mRNA to perisynaptic processes.","method":"Northern blotting (poly(A) tail analysis), co-immunoprecipitation of Fabp7 mRNA with CPEB1 from astrocyte extracts, Xenopus oocyte maturation reporter assay (CPE function), in situ hybridization, subcellular fractionation","journal":"The Journal of neuroscience","confidence":"High","confidence_rationale":"Tier 1–2 — reciprocal co-IP, functional CPE assay in Xenopus, and subcellular localization with functional consequence; multiple orthogonal methods","pmids":["22279223"],"is_preprint":false},{"year":2012,"finding":"FABP7 is a direct binding target of the neural stem cell-specific fluorescent probe CDr3 (a BODIPY derivative), identified by proteomic analysis; CDr3 binds FABP7 in the cytoplasm of living neural stem cells and can be used to isolate FABP7-high cells with neural stem cell properties.","method":"High-throughput fluorescence library screening, proteomic identification of binding target, live cell imaging, FACS isolation, neurosphere formation and differentiation assays","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 1–2 — proteomic identification of FABP7 as CDr3 binding target with functional validation of sorted cells; multiple orthogonal methods","pmids":["22689954"],"is_preprint":false},{"year":2012,"finding":"PAX6 directly transactivates the FABP7 proximal promoter; PAX6 knockdown in PAX6-positive malignant glioma cells reduces FABP7 levels, and a PAX6-responsive element was mapped to -862 to -1033 bp upstream of FABP7 by sequential deletion and gel shift/supershift assays.","method":"CAT reporter gene assay, sequential promoter deletion analysis, gel shift and supershift assays, PAX6 siRNA knockdown","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 1–2 — direct promoter transactivation, deletion mapping, and gel shift; single lab","pmids":["22583899"],"is_preprint":false},{"year":2013,"finding":"FABP7 interacts with model membranes through its portal region (helices A1 and A2 and connecting loop), delivering polyunsaturated fatty acids via a collisional mechanism; site-directed mutagenesis and ESR spectroscopy showed that portal region residues undergo structural changes upon membrane interaction, with residues pointing outward decreasing in mobility and inner residues increasing in mobility to facilitate FA delivery.","method":"Site-directed mutagenesis, electron spin resonance (ESR) spectroscopy with spin-labeled protein mutants and lipid probes, lipidic micelle model membranes","journal":"PloS one","confidence":"High","confidence_rationale":"Tier 1 — reconstituted in vitro system with mutagenesis and biophysical spectroscopy; direct structural-mechanistic insight","pmids":["23555925"],"is_preprint":false},{"year":2013,"finding":"FABP7 and FABP5 are differentially expressed in oligodendrocyte lineage cells: FABP7 is expressed in NG2+/PDGFRα+ oligodendrocyte progenitor cells (OPCs) while FABP5 marks mature oligodendrocytes; FABP7-KO OPCs show decreased proliferation and reduced differentiation into O4+ oligodendrocytes.","method":"Immunofluorescence co-staining with lineage markers in vivo and in vitro, BrdU proliferation assay, FABP7-KO and FABP5-KO OPC cultures, oligodendrocyte differentiation medium","journal":"Cell and tissue research","confidence":"High","confidence_rationale":"Tier 2 — KO with defined cellular phenotypes, replicated in vivo and in vitro with multiple markers","pmids":["24114376"],"is_preprint":false},{"year":2014,"finding":"REV-ERBα (Nr1d1) directly represses Fabp7 gene expression in the brain; loss of Rev-erbα results in Fabp7 overexpression in multiple brain areas including the hippocampal subgranular zone, leading to increased proliferation of hippocampal neuronal progenitors and loss of diurnal proliferation patterns.","method":"Rev-erbα KO mouse gene expression comparison, in vitro cell proliferation and migration assays with Fabp7 manipulation and REV-ERBα activity modulation","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 — KO with defined neurogenic phenotype; single lab","pmids":["24932636"],"is_preprint":false},{"year":2014,"finding":"A distinct chimeric FABP7 isoform (LTR2-FABP7) is ectopically expressed in a subset of diffuse large B-cell lymphoma through activation of an endogenous retroviral LTR2 promoter; this isoform is required for DLBCL cell line proliferation and growth.","method":"Whole transcriptome reanalysis, RT-PCR confirmation in DLBCL cell lines, in vitro siRNA knockdown with proliferation readout","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 — in vitro loss-of-function with proliferation readout; single lab","pmids":["25114248"],"is_preprint":false},{"year":2015,"finding":"Astrocyte-expressed FABP7 regulates dendritic morphology and excitatory synaptic function of cortical neurons; FABP7 KO astrocytes cause aberrant dendritic morphology, decreased spine density, reduced excitatory synapse number, and decreased mEPSC amplitude and frequency in mPFC pyramidal neurons; transplantation of WT astrocytes into the mPFC of KO mice partially rescued behavioral impairments.","method":"Fabp7 KO mice, Golgi staining, primary co-culture of neurons with KO astrocytes, conditioned medium experiments, whole-cell voltage-clamp recording (mEPSC), astrocyte transplantation","journal":"Glia","confidence":"High","confidence_rationale":"Tier 1–2 — multiple orthogonal methods (electrophysiology, morphology, co-culture, transplantation rescue) establishing astrocytic FABP7 as regulator of neuronal synaptic function","pmids":["26296243"],"is_preprint":false},{"year":2016,"finding":"DHA stimulates FABP7 expression in astrocytes via a PI3K/AKT-PPARγ axis; FABP7 then interacts physically with PPARγ (detected as protein-protein complex), displacing CDK5-PPARγ complex and leading to increased GFAP expression; FABP7 silencing suppresses DHA-induced GFAP upregulation.","method":"Primary rat brain astrocyte cultures, siRNA knockdown, PI3K/AKT and PPARγ inhibitor treatments, co-immunoprecipitation (FABP7-PPARγ and CDK5-PPARγ complexes), PPARγ-responsive element reporter assay","journal":"Journal of neurochemistry","confidence":"Medium","confidence_rationale":"Tier 2 — co-IP of FABP7-PPARγ interaction plus siRNA phenotype; single lab","pmids":["27787894"],"is_preprint":false},{"year":2017,"finding":"FABP7 (Fabp7) is required for normal sleep across phylogenetically disparate species; the FABP7.T61M missense mutation is associated with fragmented sleep in humans and recapitulated in mice and Drosophila; transgenic flies expressing FABP7.T61M in astrocytes show fragmented sleep, establishing FABP7 as part of a conserved astrocytic lipid-signaling pathway regulating sleep.","method":"Human sleep phenotyping (missense mutation association), Fabp7-deficient mice sleep analysis (EEG/EMG), Drosophila transgenic lines expressing FABP7.T61M in glia (sleep monitoring)","journal":"Science advances","confidence":"High","confidence_rationale":"Tier 2 — conserved across three species with specific missense mutation; multiple independent model systems establish causal role","pmids":["28435883"],"is_preprint":false},{"year":2018,"finding":"FABP7 can be regulated by PKC and the MAPK/ERK1/2 pathway in melanoma cells (PMA or MEK1 inhibitor downregulates FABP7); siRNA knockdown of FABP7 decreases melanoma cell proliferation and invasion without affecting apoptosis.","method":"PMA and MEK1 inhibitor (PD98059) treatment, siRNA knockdown, proliferation and invasion assays in human melanoma cell lines","journal":"BMC cancer","confidence":"Medium","confidence_rationale":"Tier 2 — pharmacological pathway manipulation plus siRNA with defined phenotype; single lab","pmids":["18826602"],"is_preprint":false},{"year":2018,"finding":"Glial FABP7 in hypothalamic astrocytes/tanycytes modulates neuronal leptin sensitivity; FABP7-KO mice show enhanced leptin-induced activation of ARC neurons (increased pSTAT3+ cells) and reduced weight gain on high-fat diet; primary FABP7-KO astrocytes display lower ERK phosphorylation after leptin treatment.","method":"FABP7 KO mice, diet-induced obesity model, leptin injection, immunohistochemistry (pSTAT3), primary astrocyte cultures with leptin treatment (ERK phosphorylation)","journal":"Molecular neurobiology","confidence":"Medium","confidence_rationale":"Tier 2 — in vivo KO with defined neuroendocrine phenotype plus in vitro signaling; single lab","pmids":["29623545"],"is_preprint":false},{"year":2019,"finding":"FABP7 drives metabolic reprogramming in HER2+ breast cancer brain metastasis by supporting a glycolytic phenotype and lipid droplet storage; FABP7 is required for upregulation of integrin-Src and VEGFA pathways and for in vivo tumor growth in the brain microenvironment.","method":"FABP7 knockdown and overexpression in HER2+ breast cancer cells, in vitro metabolic assays, in vivo intracranial xenograft model, pathway analysis","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 — KO/OE with in vivo xenograft plus metabolic and pathway analysis; single lab","pmids":["31324889"],"is_preprint":false},{"year":2019,"finding":"FABP7 protects astrocytes from ROS toxicity through lipid droplet (LD) formation; FABP7-KO astrocytes show significantly decreased LD accumulation, elevated ROS toxicity, impaired thioredoxin signaling, and activation of pro-apoptotic p38 MAPK and SAPK/JNK pathways; FABP7 overexpression in glioma cells increases LD accumulation and antioxidant enzyme expression.","method":"FABP7-KO primary mouse astrocytes, ROS induction, LD quantification, Western blot (TRX, PRX1, p38 MAPK, SAPK/JNK, caspase-3), NAC rescue, FABP7 overexpression in U87 cells","journal":"Molecular neurobiology","confidence":"High","confidence_rationale":"Tier 2 — KO and OE with multiple orthogonal readouts (LD, ROS, signaling, apoptosis, rescue); mechanistically defined","pmids":["30680690"],"is_preprint":false},{"year":2020,"finding":"FABP7 overexpression in astrocytes induces an NF-κB-driven pro-inflammatory response that is detrimental for motor neuron survival; silencing FABP7 in astrocytes from symptomatic hSOD1-expressing mice decreases inflammatory markers and reduces toxicity toward co-cultured motor neurons; a ligand-binding impaired mutant FABP7 does not induce NF-κB activation.","method":"FABP7 overexpression in non-transgenic astrocytes, astrocyte-motor neuron co-culture, siRNA knockdown, NF-κB reporter assay, hSOD1 transgenic mouse astrocyte cultures, mutant FABP7 (ligand-binding impaired)","journal":"Glia","confidence":"High","confidence_rationale":"Tier 2 — gain and loss-of-function with mechanistic NF-κB pathway placement and mutant FABP7 control; multiple orthogonal methods","pmids":["32619303"],"is_preprint":false},{"year":2020,"finding":"FABP7 interacts with ATP-citrate lyase (ACLY) in the nucleus and is important for acetyl-CoA metabolism; the FABP7-ACLY interaction modulates nuclear histone acetylation and thereby epigenetically regulates caveolin-1 expression in astrocytes and glioma cells.","method":"Co-immunoprecipitation (FABP7-ACLY interaction), FABP7-KO primary astrocytes, NIH-3T3 gain-of-function model, histone acetylation assay, caveolin-1 promoter analysis","journal":"Molecular neurobiology","confidence":"High","confidence_rationale":"Tier 2 — co-IP identifying ACLY as binding partner, KO and OE with epigenetic readout; multiple orthogonal methods","pmids":["32812201"],"is_preprint":false},{"year":2020,"finding":"FABP7 is required for optimal OPC differentiation during developmental myelination but is dispensable for remyelination; Fabp7 knockdown reduces OPC differentiation in vitro and Fabp7 KO mice show a transient delay in developmental myelination that resolves before adulthood.","method":"Fabp7 siRNA knockdown in OPC cultures, Fabp7 KO mouse developmental myelination analysis, focal demyelination model (remyelination assay)","journal":"Glia","confidence":"Medium","confidence_rationale":"Tier 2 — in vitro KD and in vivo KO with specific myelination phenotype; single lab","pmids":["32017258"],"is_preprint":false},{"year":2021,"finding":"Rev-erbα directly binds the Fabp7 promoter in multiple brain areas (hippocampus, hypothalamus, VTA) as shown by ChIP-seq, and Fabp7 gene expression is specifically and robustly upregulated (>6-fold across all brain regions) in Rev-erbα KO mice, establishing Rev-erbα as a direct transcriptional repressor of Fabp7.","method":"ChIP-seq (Rev-erbα binding at Fabp7 promoter), Rev-erbα KO mouse, quantitative mRNA analysis across multiple brain areas","journal":"Current research in neurobiology","confidence":"High","confidence_rationale":"Tier 1–2 — ChIP-seq direct binding evidence plus in vivo KO; mechanistically defined","pmids":["34056625"],"is_preprint":false},{"year":2021,"finding":"Ligand-bound FABP7 drives melanoma cell proliferation via activation of Wnt/β-catenin signaling; wild-type FABP7 overexpression increases Wnt/β-catenin activity (luciferase reporter), cyclin D1 expression, and proliferation, while a FA-binding site mutant FABP7 abrogates these effects; pharmacological inhibition of FABP7 with MF6 suppresses these responses.","method":"FABP7 siRNA knockdown and OE with wild-type vs. mutant FABP7, Wnt/β-catenin luciferase reporter assay, proliferation and migration assay, MF6 pharmacological inhibition","journal":"Pharmaceutical research","confidence":"High","confidence_rationale":"Tier 1–2 — reporter assay, ligand-binding mutant control, pharmacological inhibition; multiple orthogonal methods establishing ligand-binding dependence","pmids":["33646504"],"is_preprint":false},{"year":2021,"finding":"FABP7 facilitates uptake of DHA in GBM neural stem-like cells; FABP7 knockdown reduces DHA incorporation into GBM cells and diminishes DHA-induced inhibition of cell migration.","method":"FABP7 knockdown in patient-derived GBM neurosphere cultures, fatty acid composition analysis (lipidomics), migration assay","journal":"Nutrients","confidence":"Medium","confidence_rationale":"Tier 2 — KD with specific FA uptake and functional migration readout; single lab","pmids":["34444824"],"is_preprint":false},{"year":2021,"finding":"Nuclear FABP7 promotes glioblastoma cell proliferation in IDH1-wild-type glioma through caveolae formation; FABP7wt overexpression increases caveolin-1 expression and caveolae/caveosome formation via elevated H3K27ac on the caveolin-1 promoter through ACLY-dependent nuclear acetyl-CoA regulation; mutant FABP7 (FA-binding impaired) abrogates these effects in vitro and in xenograft models.","method":"FABP7wt and FABP7mut overexpression in U87 cells, caveolae/caveosome visualization, H3K27ac ChIP on caveolin-1 promoter, nuclear acetyl-CoA measurement, in vivo xenograft, patient GBM tissue analysis","journal":"Molecular oncology","confidence":"High","confidence_rationale":"Tier 1–2 — ChIP, mutant control, in vivo xenograft, nuclear acetyl-CoA measurement; multiple orthogonal methods","pmids":["34716958"],"is_preprint":false},{"year":2021,"finding":"NMR and molecular dynamics simulations demonstrate that FABP7 has high conformational heterogeneity that is substantially reduced upon fatty acid ligand binding; DHA binding leads to chemical shift perturbations in residues near the nuclear localization signal, suggesting a mechanism for differential nuclear vs. cytoplasmic transport depending on ligand identity; ligand binding is resistant to mutations in polar binding pocket residues.","method":"NMR spectroscopy, multiscale molecular dynamics simulations, site-directed mutagenesis of binding pocket residues, biophysical binding assays","journal":"Biophysical journal","confidence":"High","confidence_rationale":"Tier 1 — NMR plus MD simulations plus mutagenesis providing structural-mechanistic insight into ligand-directed transport","pmids":["36698315"],"is_preprint":false},{"year":2021,"finding":"Crystal structure of human FABP7 complexed with palmitic acid (a saturated FA) at 1.6 Å resolution reveals a U-shaped binding conformation; the carboxylate of palmitic acid interacts with Tyr129, Arg127, and via water bridge with Arg107 and Thr54, while the aliphatic chain is stabilized by hydrophobic interactions with Met21, Leu24, Thr30, Thr37, Pro39, Phe58, and Asp77; PA, OA, and DHA adopt distinct binding conformations in the pocket.","method":"X-ray crystallography (1.6 Å resolution), structural comparison with OA- and DHA-bound FABP7 and other FABP family members","journal":"Acta crystallographica. Section D, Structural biology","confidence":"High","confidence_rationale":"Tier 1 — crystal structure with detailed binding interactions characterized at atomic resolution","pmids":["34196621"],"is_preprint":false},{"year":2022,"finding":"Oleic acid-bound FABP7 drives glioma cell proliferation by promoting nuclear localization of the FABP7-OA complex, inducing nuclear lipid droplet (nLD) formation, increasing colocalization of nLD with PML nuclear bodies, and enhancing histone acetylation-dependent transcription of proliferation-related genes; FA-binding site mutant FABP7 abrogates all these effects.","method":"OA treatment of FABP7-expressing cells, FABP7 nuclear localization imaging, nLD visualization, PML body co-localization, histone acetylation assay, mRNA profiling, FABP7-KO and FABP7-mutant overexpression controls","journal":"The FEBS journal","confidence":"High","confidence_rationale":"Tier 1–2 — mechanistic chain from ligand binding to nuclear LD formation to histone acetylation to gene expression, with mutant FABP7 control; multiple orthogonal methods","pmids":["36325660"],"is_preprint":false},{"year":2022,"finding":"FABP7 promotes NSCLC metastasis by competitively inhibiting the interaction between β-catenin and its cytoplasmic degradation complex, thereby repressing phosphorylation-dependent ubiquitination and degradation of β-catenin and activating canonical Wnt signaling.","method":"FABP7 KD and OE in NSCLC cell lines, in vivo metastasis model, co-immunoprecipitation (β-catenin with degradation complex), β-catenin phosphorylation and ubiquitination assays","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 — co-IP showing FABP7 competition with β-catenin degradation complex; single lab","pmids":["35269427"],"is_preprint":false},{"year":2023,"finding":"Wild-type FABP7 overexpression induces an NF-κB-driven inflammatory response in human iPSC-derived astrocytes (identified by RNA-seq as top biological process); a ligand-binding impaired mutant FABP7 does not activate NF-κB, demonstrating that FABP7's pro-inflammatory function requires its fatty acid-binding activity; amyloid-β treatment induces FABP7 upregulation in primary hippocampal astrocytes.","method":"FABP7 OE in human iPSC-derived astrocytes, whole transcriptome RNA-seq, Gene Ontology analysis, NF-κB reporter assay, ligand-binding mutant FABP7 control, Aβ treatment of primary astrocytes, APP/PS1 mouse immunostaining","journal":"GeroScience","confidence":"High","confidence_rationale":"Tier 1–2 — RNA-seq with OE/mutant comparison, NF-κB reporter, and ligand-binding mutant control; multiple orthogonal methods","pmids":["37688656"],"is_preprint":false},{"year":2023,"finding":"FABP7 forms hetero-aggregates with α-synuclein (αSyn) that exhibit stronger toxicity than αSyn aggregates alone; injected FABP7/αSyn hetero-aggregates selectively accumulate in oligodendrocytes and Purkinje neurons causing cerebellar dysfunction; epsin-2 regulates FABP7/αSyn hetero-aggregate propagation via clathrin-dependent endocytosis, and epsin-2 knockdown decreases αSyn aggregate accumulation and improves motor performance.","method":"MSA mouse models (PLP-hαSyn, FABP7/αSyn hetero-aggregate injection), co-aggregation assays, AAV5-dependent epsin-2 knockdown, histology, motor function testing, bioinformatic analysis of MSA patient whole blood","journal":"Brain : a journal of neurology","confidence":"High","confidence_rationale":"Tier 2 — direct in vivo hetero-aggregate injection, cell-type selective accumulation, and epsin-2 epistasis with rescue; multiple methods","pmids":["37082980"],"is_preprint":false},{"year":2023,"finding":"FABP7 binds oleic acid and DHA micelles through its portal region residues; NMR and molecular dynamics simulations reveal that binding to micelles occurs through the same portal region as membrane binding, and simulations capture fatty acid dissociation from membranes directly entering FABP7's binding pocket.","method":"NMR spectroscopy, multiscale molecular dynamics simulations, biophysical binding assays with OA and DHA micelles","journal":"Biophysical journal","confidence":"High","confidence_rationale":"Tier 1 — direct NMR plus MD simulations capturing atomic-level binding mechanism; multiple complementary biophysical methods","pmids":["36698315"],"is_preprint":false},{"year":2024,"finding":"FABP7 deficiency in iPSC-derived cerebral organoids from normocephalic ASD individuals causes premature neural differentiation of neural stem cells; altered phosphorylation of MEK1/2 (downstream of FABP7) was detected, and regulation of the FABP7/MEK pathway reversed improper neural differentiation; Fabp7 knockdown and MEK2-overexpressing mice exhibit repetitive stereotyped behaviors and social defects.","method":"iPSC-derived cerebral organoids from ASD patients, single-cell RNA-seq (time series), FABP7 loss-of-function rescue experiments via FABP7/MEK pathway modulation, Fabp7 KD mice behavioral phenotyping (open field, social interaction)","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"High","confidence_rationale":"Tier 2 — human organoid model + pathway rescue + in vivo KD mouse phenotype; multiple orthogonal methods across human and mouse","pmids":["39556706"],"is_preprint":false},{"year":2025,"finding":"FABP7 in hepatic macrophages modulates M2 polarization via PPARγ and its target genes (CCL17, TGF-β); FABP7-deficient macrophages display decreased PPARγ activity, reduced fibrotic response of myofibroblasts, and decreased CD4+ T-cell migration into liver; in vitro, IL-4-stimulated FABP7-deficient macrophages show reduced CCL-17 and TGF-β, effects blocked by PPARγ inhibitor.","method":"FABP7 KO in CCl4-induced hepatic fibrosis model, in vitro macrophage polarization assays, PPARγ inhibitor treatment, co-culture of macrophages with CD4+ T cells and hepatic stellate cells","journal":"Journal of immunology research","confidence":"Medium","confidence_rationale":"Tier 2 — KO in vivo model plus in vitro mechanistic validation with PPARγ inhibitor; single lab","pmids":["40017805"],"is_preprint":false},{"year":2025,"finding":"Extracellular FABP7 induces a pro-inflammatory phenotype in monocytes via increased glycolysis, upregulating CD16, CD80 and IL-1β; FABP7-induced gene expression in monocytes reflects enhanced inflammation, chemotaxis, and glucose metabolism.","method":"In vitro FABP7 treatment of monocytes, flow cytometry (CD16, CD80), ELISA (IL-1β), transcriptomics, glycolysis assays; patient serum/CSF FABP7 measurement","journal":"Nature communications","confidence":"Medium","confidence_rationale":"Tier 2 — in vitro mechanistic experiment with multiple readouts establishing glycolytic switch; single lab but published in high-impact journal","pmids":["40595541"],"is_preprint":false},{"year":2025,"finding":"FABP7 silencing in astrocytes decreases NF-κB-p65 nuclear translocation and NF-κB reporter activity in response to multiple inflammatory stimuli, reduces astrocyte toxicity toward motor neurons, and reduces glial activation in vivo after LPS administration; whole transcriptome RNA-seq confirms attenuation of NF-κB-dependent transcriptional response.","method":"FABP7 siRNA in primary mouse and human iPSC-derived astrocytes, NF-κB reporter assay, NF-κB-p65 nuclear translocation imaging, astrocyte-motor neuron co-culture, in vivo astrocytic FABP7 knockdown in LPS-treated mice, RNA-seq","journal":"Glia","confidence":"High","confidence_rationale":"Tier 2 — multiple cell types (mouse, human iPSC-derived), in vivo validation, RNA-seq; mechanistically placed in NF-κB pathway","pmids":["40251832"],"is_preprint":false},{"year":2026,"finding":"YRDC-catalyzed tRNA t6A modification drives codon-biased translation of FABP7 mRNA; elevated FABP7 induces lipid droplet accumulation that sequesters TMZ-induced ROS to confer chemoresistance in glioblastoma; YRDC inhibition suppresses FABP7 translation and lipid droplets, synergizing with TMZ in vitro and in orthotopic xenografts.","method":"YRDC KD/OE, polysome profiling/ribosome profiling (codon-biased translation), lipid droplet quantification, ROS assays, in vitro and in vivo (PDX) TMZ resistance models, YRDC inhibitor (HY-Q66655) virtual screening and functional validation","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 — mechanistic chain from tRNA modification to FABP7 translation to LD to chemoresistance; single lab but multiple orthogonal methods","pmids":["42014887"],"is_preprint":false}],"current_model":"FABP7 is an astrocyte/radial glia-enriched intracellular lipid chaperone that binds long-chain polyunsaturated fatty acids (especially DHA and arachidonic acid) through a defined binding pocket and delivers them via a portal-region-mediated collisional mechanism to membranes or to the nucleus, where ligand identity dictates subcellular trafficking; in the nucleus FABP7 interacts with ACLY to regulate acetyl-CoA levels and histone acetylation, epigenetically controlling genes such as caveolin-1, and activates NF-κB-driven inflammatory responses in a ligand-binding-dependent manner; at the cellular level FABP7 maintains neural stem/progenitor cell proliferation downstream of Pax6, regulates astrocyte-dependent dendritic morphology and excitatory synaptic function, modulates sleep across species through astrocytic lipid signaling, promotes lipid droplet formation to protect against ROS, and in cancer contexts drives proliferation and invasion through Wnt/β-catenin, MEK/ERK, and glycolytic reprogramming pathways."},"narrative":{"teleology":[{"year":1994,"claim":"The discovery that FABP7 (BLBP) is a brain-specific lipid-binding protein localizing to both nucleus and cytoplasm of radial glia, and that its antibody-mediated blockade disrupts the radial glial fiber system, established FABP7 as a functional mediator of glial differentiation rather than a passive lipid carrier.","evidence":"Immunoelectron microscopy for subcellular localization, anti-BLBP antibody blockade in primary brain cell cultures","pmids":["8161459"],"confidence":"High","gaps":["Identity of the endogenous lipid ligand was unknown","Mechanism linking lipid binding to radial glial fiber formation was not defined","Nuclear function was not explored"]},{"year":2005,"claim":"Placing FABP7 downstream of Pax6 and showing that its knockdown causes premature neuronal differentiation established FABP7 as a transcriptionally regulated effector maintaining neural stem/progenitor cell proliferation.","evidence":"In vivo electroporation of siRNA in embryonic rat cortex with BrdU proliferation assay; Pax6 overexpression inducing Fabp7","pmids":["16237179"],"confidence":"High","gaps":["Whether FABP7 is a direct versus indirect Pax6 target was not resolved at this stage","Downstream lipid-dependent effectors of proliferation maintenance were unknown"]},{"year":2007,"claim":"Fabp7 knockout mice exhibiting decreased prepulse inhibition and disrupted neurogenesis linked FABP7 to NMDA receptor-related circuits and sensorimotor gating, broadening its role from development to postnatal brain function.","evidence":"QTL analysis, Fabp7 KO mouse behavioral phenotyping, BrdU neurogenesis assay, quantitative complementation","pmids":["18001149"],"confidence":"High","gaps":["Whether the PPI deficit is cell-autonomous to glia or neurons was unclear","Molecular pathway from FABP7 to NMDA receptor signaling was not defined"]},{"year":2008,"claim":"The observation that Fabp7 mRNA and protein undergo diurnal oscillations in adult astrocytes, peaking at opposite phases, suggested post-transcriptional regulation and a role in circadian brain physiology.","evidence":"RNA and protein time-course analysis across 24 h in adult mouse brain by in situ hybridization and immunoblot","pmids":["18286188"],"confidence":"Medium","gaps":["Transcriptional versus post-transcriptional basis of oscillation was not resolved","Functional consequence of diurnal FABP7 cycling was not tested"]},{"year":2012,"claim":"Multiple studies converged to show that FABP7 mRNA undergoes CPEB1-dependent polyadenylation for perisynaptic localization in astrocytes, that PAX6 directly transactivates the FABP7 promoter, and that FABP7 maintains neural stem cell proliferation in the adult hippocampus, integrating transcriptional, post-transcriptional, and stem cell biology dimensions.","evidence":"Co-IP of Fabp7 mRNA with CPEB1, Xenopus CPE reporter assay, PAX6 promoter deletion/gel shift, Fabp7 KO hippocampal BrdU assays","pmids":["22279223","22583899","22581784"],"confidence":"High","gaps":["Whether CPEB1-dependent translation directly regulates perisynaptic lipid metabolism was not shown","Full set of transcription factors controlling FABP7 expression was incomplete"]},{"year":2013,"claim":"Biophysical and structural studies demonstrated that FABP7 delivers fatty acids to membranes via a portal-region collisional mechanism, with helices αI/αII undergoing conformational rearrangement, providing the first mechanistic model for FABP7-mediated lipid transfer.","evidence":"Site-directed mutagenesis, ESR spectroscopy with spin-labeled mutants and lipid probes","pmids":["23555925"],"confidence":"High","gaps":["Whether the collisional mechanism operates identically at nuclear versus plasma membranes was untested","Kinetic parameters of transfer for different FA species were not measured"]},{"year":2014,"claim":"ChIP and KO data established REV-ERBα as a direct transcriptional repressor of Fabp7 in the brain, connecting clock machinery to FABP7-driven progenitor proliferation and providing a molecular link between circadian regulation and neurogenesis.","evidence":"Rev-erbα KO mouse, promoter ChIP-seq, cell proliferation assays","pmids":["24932636","34056625"],"confidence":"High","gaps":["Whether REV-ERBα repression accounts for the full diurnal FABP7 oscillation was not resolved","Other circadian regulators of FABP7 were not excluded"]},{"year":2015,"claim":"Demonstrating that FABP7-KO astrocytes impair dendritic morphology, spine density, and excitatory synaptic transmission of co-cultured neurons — with partial rescue by WT astrocyte transplantation — established FABP7 as an astrocytic regulator of neuronal circuit structure and function.","evidence":"Fabp7 KO mice, Golgi staining, neuron-astrocyte co-culture, mEPSC recording, astrocyte transplantation in mPFC","pmids":["26296243"],"confidence":"High","gaps":["The secreted or contact-dependent astrocytic signal was not identified","Whether specific FABP7-transported lipids mediate the synaptic effects was unknown"]},{"year":2017,"claim":"The T61M missense variant's association with fragmented sleep in humans, mice, and Drosophila — with astrocyte-specific expression in flies — established FABP7 as part of a phylogenetically conserved astrocytic lipid-signaling pathway regulating sleep.","evidence":"Human genotype-phenotype association, Fabp7 KO mouse EEG/EMG, transgenic Drosophila expressing FABP7.T61M in glia","pmids":["28435883"],"confidence":"High","gaps":["Downstream lipid signals mediating sleep consolidation were not identified","Whether the T61M mutation alters ligand binding specificity or affinity was not structurally resolved"]},{"year":2019,"claim":"FABP7 was shown to promote lipid droplet formation that protects astrocytes from ROS toxicity via thioredoxin signaling, and to support glycolytic reprogramming in HER2+ breast cancer brain metastasis, linking its lipid-shuttling function to metabolic stress responses.","evidence":"FABP7 KO astrocytes with ROS induction and LD quantification; FABP7 KD/OE in HER2+ cells with metabolic assays and intracranial xenograft","pmids":["30680690","31324889"],"confidence":"High","gaps":["Whether LD-mediated ROS protection requires specific FA species was untested","Direct lipid cargo in cancer metabolic reprogramming was not identified"]},{"year":2020,"claim":"Discovery that FABP7 interacts with ACLY in the nucleus and modulates histone acetylation (including H3K27ac at the caveolin-1 promoter) revealed an epigenetic effector function, while ligand-binding-dependent NF-κB activation in astrocytes linked FABP7 to neuroinflammation in ALS models.","evidence":"Co-IP of FABP7–ACLY, histone acetylation ChIP, FABP7 OE/KO in astrocytes, NF-κB reporter, ligand-binding mutant control, hSOD1 astrocyte co-culture","pmids":["32812201","32619303"],"confidence":"High","gaps":["Whether ACLY interaction requires a specific lipid ligand was not resolved","Structural basis of FABP7–ACLY interaction was unknown","Whether NF-κB activation is direct or mediated through ACLY/acetyl-CoA was not distinguished"]},{"year":2021,"claim":"Crystal structures of FABP7 with different fatty acids and NMR/MD studies showing ligand-dependent conformational changes near the NLS provided a structural explanation for how lipid identity directs FABP7's nuclear versus cytoplasmic distribution, and ligand-bound FABP7 was shown to activate Wnt/β-catenin signaling in melanoma.","evidence":"X-ray crystallography at 1.6 Å, NMR spectroscopy, MD simulations, mutagenesis; Wnt/β-catenin reporter with WT vs. FA-binding-site mutant FABP7, MF6 pharmacological inhibition","pmids":["34196621","36698315","33646504"],"confidence":"High","gaps":["Structural basis for NLS exposure upon specific ligand binding remains at simulation level","Whether Wnt activation is direct or through β-catenin degradation complex competition was not fully resolved at this point"]},{"year":2022,"claim":"Oleic acid-bound FABP7 was shown to drive nuclear lipid droplet formation colocalizing with PML bodies and enhancing histone acetylation-dependent proliferative gene expression, providing a complete mechanistic chain from ligand binding through nuclear LD to epigenetic transcriptional control.","evidence":"FABP7 OE with OA, nuclear LD and PML body colocalization imaging, histone acetylation assay, mRNA profiling, FABP7 FA-binding mutant control","pmids":["36325660"],"confidence":"High","gaps":["Whether nuclear LD formation requires ACLY-dependent acetyl-CoA was not directly tested in this study","PML body functional requirement was not confirmed by PML loss-of-function"]},{"year":2023,"claim":"FABP7's pro-inflammatory NF-κB activation was validated in human iPSC-derived astrocytes with RNA-seq and shown to require fatty acid binding, while FABP7 was also found to form toxic hetero-aggregates with α-synuclein that accumulate in oligodendrocytes via epsin-2-dependent endocytosis, extending FABP7's pathological roles to Alzheimer's and multiple system atrophy.","evidence":"FABP7 OE in iPSC astrocytes with RNA-seq and ligand-binding mutant; FABP7/αSyn hetero-aggregate injection in MSA mouse models, AAV5-epsin-2 KD rescue","pmids":["37688656","37082980"],"confidence":"High","gaps":["Which specific FA species drive NF-κB activation in human astrocytes was not determined","Whether FABP7/αSyn aggregation is relevant in sporadic Parkinson's disease was not tested"]},{"year":2024,"claim":"FABP7 deficiency in ASD patient-derived cerebral organoids caused premature neural differentiation rescued by MEK pathway modulation, and Fabp7-KD mice exhibited ASD-like behaviors, establishing FABP7/MEK as a functional axis in autism-relevant neural development.","evidence":"iPSC-derived cerebral organoids, scRNA-seq time series, FABP7/MEK pathway rescue, Fabp7 KD mouse behavioral phenotyping","pmids":["39556706"],"confidence":"High","gaps":["Whether FABP7 directly activates MEK or acts through an intermediate lipid signal was not resolved","Genetic variants in FABP7 causative for ASD in families were not identified"]},{"year":2025,"claim":"Extracellular FABP7 was shown to reprogram monocyte metabolism toward glycolysis and inflammation, while intracellular FABP7 in hepatic macrophages modulates PPARγ-dependent M2 polarization, and astrocytic FABP7 silencing attenuates NF-κB-p65 nuclear translocation in vivo, consolidating FABP7 as a lipid-dependent inflammatory mediator across cell types.","evidence":"In vitro monocyte treatment with extracellular FABP7, FABP7 KO in hepatic fibrosis model with PPARγ inhibitor, astrocytic FABP7 siRNA in vivo with LPS challenge and RNA-seq","pmids":["40595541","40017805","40251832"],"confidence":"High","gaps":["Receptor or uptake mechanism for extracellular FABP7 on monocytes is unknown","Whether PPARγ and NF-κB pathways are independently or sequentially activated by FABP7 is unresolved"]},{"year":null,"claim":"Key unresolved questions include: the identity of specific lipid species that dictate FABP7's nuclear versus cytoplasmic function in vivo; the structural basis of the FABP7–ACLY interaction; the receptor or mechanism for extracellular FABP7 uptake; and whether FABP7-dependent sleep regulation operates through the same NF-κB/epigenetic axis identified in neuroinflammation.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of FABP7–ACLY complex exists","Lipid species specificity for each downstream pathway is undefined in vivo","Mechanism linking FABP7 to sleep at the molecular level is uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008289","term_label":"lipid binding","supporting_discovery_ids":[0,10,28,29,34]},{"term_id":"GO:0140104","term_label":"molecular carrier activity","supporting_discovery_ids":[10,34]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[21,22,25,31,32,38]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,22,27,28,30]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0,8]},{"term_id":"GO:0005811","term_label":"lipid droplet","supporting_discovery_ids":[20,30,39]},{"term_id":"GO:0005576","term_label":"extracellular region","supporting_discovery_ids":[37]}],"pathway":[{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[1,9,22,27,30]},{"term_id":"R-HSA-4839726","term_label":"Chromatin organization","supporting_discovery_ids":[22,27,30]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[15,21,25,31,32,38]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[0,1,6,11,35]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[21,32,36,37,38]},{"term_id":"R-HSA-1430728","term_label":"Metabolism","supporting_discovery_ids":[19,20,26,39]}],"complexes":[],"partners":["ACLY","CPEB1","PPARG","PAX6","NR1D1","SNCA","CTNNB1"],"other_free_text":[]},"mechanistic_narrative":"FABP7 is an intracellular fatty acid-binding protein that functions as a lipid chaperone in radial glia, astrocytes, and neural stem/progenitor cells, coupling fatty acid transport to nuclear signaling, epigenetic regulation, and inflammatory responses. FABP7 binds long-chain polyunsaturated fatty acids (DHA, oleic acid, arachidonic acid) in a β-barrel pocket and delivers them to membranes via a portal-region-mediated collisional mechanism; ligand identity dictates conformational changes near the nuclear localization signal, directing subcellular trafficking of the FABP7–fatty acid complex to the nucleus where it interacts with ACLY to regulate acetyl-CoA levels and histone acetylation at targets including caveolin-1 [PMID:23555925, PMID:36698315, PMID:34196621, PMID:32812201, PMID:36325660]. In development, FABP7 acts downstream of Pax6 and is repressed by REV-ERBα, maintaining neural stem cell proliferation and regulating oligodendrocyte progenitor differentiation; its loss causes premature neuronal differentiation, disrupted dendritic morphology, and reduced excitatory synaptic function through astrocyte-dependent mechanisms [PMID:16237179, PMID:34056625, PMID:26296243, PMID:22581784]. FABP7 activates NF-κB-driven neuroinflammation in a ligand-binding-dependent manner, promotes lipid droplet formation that sequesters reactive oxygen species, and regulates sleep through a conserved astrocytic lipid-signaling pathway disrupted by the human T61M missense variant [PMID:40251832, PMID:32619303, PMID:30680690, PMID:28435883]."},"prefetch_data":{"uniprot":{"accession":"O15540","full_name":"Fatty acid-binding protein, brain","aliases":["Brain lipid-binding protein","BLBP","Brain-type fatty acid-binding protein","B-FABP","Fatty acid-binding protein 7","Mammary-derived growth inhibitor related"],"length_aa":132,"mass_kda":14.9,"function":"B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity)","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/O15540/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/FABP7","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/FABP7","total_profiled":1310},"omim":[{"mim_id":"605168","title":"FATTY ACID-BINDING PROTEIN 5; FABP5","url":"https://www.omim.org/entry/605168"},{"mim_id":"602965","title":"FATTY ACID-BINDING PROTEIN 7; FABP7","url":"https://www.omim.org/entry/602965"},{"mim_id":"602100","title":"PBX/KNOTTED 1 HOMEOBOX 1; PKNOX1","url":"https://www.omim.org/entry/602100"},{"mim_id":"301009","title":"P ANTIGEN FAMILY, MEMBER 5; PAGE5","url":"https://www.omim.org/entry/301009"},{"mim_id":"137800","title":"GLIOMA SUSCEPTIBILITY 1; GLM1","url":"https://www.omim.org/entry/137800"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Golgi apparatus","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in some","driving_tissues":[{"tissue":"brain","ntpm":232.2},{"tissue":"retina","ntpm":162.4},{"tissue":"tongue","ntpm":186.2}],"url":"https://www.proteinatlas.org/search/FABP7"},"hgnc":{"alias_symbol":["B-FABP","BLBP"],"prev_symbol":[]},"alphafold":{"accession":"O15540","domains":[{"cath_id":"2.40.128.20","chopping":"1-127","consensus_level":"high","plddt":96.6234,"start":1,"end":127}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O15540","model_url":"https://alphafold.ebi.ac.uk/files/AF-O15540-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O15540-F1-predicted_aligned_error_v6.png","plddt_mean":96.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=FABP7","jax_strain_url":"https://www.jax.org/strain/search?query=FABP7"},"sequence":{"accession":"O15540","fasta_url":"https://rest.uniprot.org/uniprotkb/O15540.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O15540/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O15540"}},"corpus_meta":[{"pmid":"8161459","id":"PMC_8161459","title":"Brain 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localization), anti-BLBP antibody blockade in primary cell cultures (functional loss-of-function), in situ hybridization and immunocytochemistry (expression pattern)\",\n      \"journal\": \"Neuron\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — direct protein localization by immunoelectron microscopy plus functional antibody-blockade assay with defined phenotypic readout; foundational paper with 488 citations\",\n      \"pmids\": [\"8161459\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"Fabp7 is a downstream transcriptional target of Pax6 in the developing rat cortex; Fabp7 siRNA knockdown curtails neuroepithelial cell proliferation and promotes premature neuronal differentiation, demonstrating Fabp7 is required for maintenance of neuroepithelial cells.\",\n      \"method\": \"Microarray followed by quantitative PCR (expression), electroporation of siRNA in embryonic rat cortex (in vivo loss-of-function), Pax6 overexpression (gain-of-function), BrdU proliferation assay\",\n      \"journal\": \"The Journal of neuroscience\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — in vivo siRNA knockdown with specific proliferation/differentiation phenotype plus epistasis (Pax6 overexpression inducing Fabp7); replicated observations in multiple model conditions\",\n      \"pmids\": [\"16237179\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"Fabp7-deficient mice show decreased prepulse inhibition and disrupted neurogenesis in vivo, placing Fabp7 in a pathway linking NMDA receptor signaling, glial function, and sensorimotor gating; genetic complementation test supported Fabp7 as the QTL gene.\",\n      \"method\": \"QTL analysis, Fabp7 knockout mice behavioral phenotyping (PPI assay), BrdU neurogenesis assay, quantitative complementation test\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (QTL mapping, KO phenotyping, quantitative complementation, neurogenesis assay) in a single highly-cited study\",\n      \"pmids\": [\"18001149\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"PKNOX1 (PREP1), a transcription factor encoded on chromosome 21, directly binds the Pbx/POU site of the FABP7 promoter in vitro and transactivates FABP7 promoter activity in neuroblastoma cells, linking chromosome 21 gene-dosage imbalance in Down syndrome to FABP7 overexpression.\",\n      \"method\": \"Genomic inverse PCR (promoter cloning), in vitro binding assay (PKNOX1 binding to FABP7 promoter), transfection/promoter transactivation assay in neuroblastoma cells, real-time PCR\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vitro binding and promoter transactivation assays with functional context; single lab\",\n      \"pmids\": [\"12771203\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"Brain fatty acid-binding protein Fabp7 mRNA and protein levels undergo diurnal oscillations throughout adult mouse brain, with mRNA peaking during the light period and protein peaking during the dark period; this diurnal rhythm is present in astrocytes and hippocampal granule cell precursors but is absent in immature postnatal brain where astrocytes are not yet mature.\",\n      \"method\": \"RNA analysis, in situ hybridization, immunoblot (diurnal expression profiling across 24 h in adult and postnatal mouse brain)\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct measurement of mRNA and protein at multiple time points across brain regions; single lab but comprehensive\",\n      \"pmids\": [\"18286188\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"FABP7 is required for astrocyte proliferation following brain stab injury; FABP7-KO astrocytes show decreased proliferation and reduced omega-3 fatty acid incorporation, linking FABP7 to cellular fatty acid homeostasis in reactive gliosis.\",\n      \"method\": \"Mouse cortical stab injury model, Western blot, immunohistochemistry, BrdU proliferation assay in FABP7-KO vs wild-type mice, primary astrocyte culture from KO mice\",\n      \"journal\": \"Histochemistry and cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — in vivo KO model with defined proliferation phenotype plus in vitro primary astrocyte validation; multiple orthogonal methods\",\n      \"pmids\": [\"21938553\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Fabp7 and Fabp5 are differentially expressed in postnatal hippocampal neural stem/progenitor cells; Fabp7 KO reduces NSC/NPC proliferation and BrdU uptake while enhancing neuronal differentiation in the subgranular zone of the dentate gyrus.\",\n      \"method\": \"Immunofluorescence, BrdU pulse-chase assay, Fabp7 KO / Fabp5 KO / double-KO mouse analysis\",\n      \"journal\": \"Stem cells (Dayton, Ohio)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple KO genotypes with BrdU proliferation and survival assays; replicated across anterior-posterior axis\",\n      \"pmids\": [\"22581784\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"FABP7 mRNA localizes to the astrocytic perisynaptic compartment and undergoes diurnal changes in intracellular distribution; Fabp7 mRNA co-immunoprecipitates with CPEB1 from primary astrocyte extracts, and its 3'UTR contains functional cytoplasmic polyadenylation elements (CPEs) capable of regulating mRNA translation, implicating circadian/sleep-dependent polyadenylation in subcellular trafficking of Fabp7 mRNA to perisynaptic processes.\",\n      \"method\": \"Northern blotting (poly(A) tail analysis), co-immunoprecipitation of Fabp7 mRNA with CPEB1 from astrocyte extracts, Xenopus oocyte maturation reporter assay (CPE function), in situ hybridization, subcellular fractionation\",\n      \"journal\": \"The Journal of neuroscience\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — reciprocal co-IP, functional CPE assay in Xenopus, and subcellular localization with functional consequence; multiple orthogonal methods\",\n      \"pmids\": [\"22279223\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"FABP7 is a direct binding target of the neural stem cell-specific fluorescent probe CDr3 (a BODIPY derivative), identified by proteomic analysis; CDr3 binds FABP7 in the cytoplasm of living neural stem cells and can be used to isolate FABP7-high cells with neural stem cell properties.\",\n      \"method\": \"High-throughput fluorescence library screening, proteomic identification of binding target, live cell imaging, FACS isolation, neurosphere formation and differentiation assays\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — proteomic identification of FABP7 as CDr3 binding target with functional validation of sorted cells; multiple orthogonal methods\",\n      \"pmids\": [\"22689954\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"PAX6 directly transactivates the FABP7 proximal promoter; PAX6 knockdown in PAX6-positive malignant glioma cells reduces FABP7 levels, and a PAX6-responsive element was mapped to -862 to -1033 bp upstream of FABP7 by sequential deletion and gel shift/supershift assays.\",\n      \"method\": \"CAT reporter gene assay, sequential promoter deletion analysis, gel shift and supershift assays, PAX6 siRNA knockdown\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1–2 — direct promoter transactivation, deletion mapping, and gel shift; single lab\",\n      \"pmids\": [\"22583899\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"FABP7 interacts with model membranes through its portal region (helices A1 and A2 and connecting loop), delivering polyunsaturated fatty acids via a collisional mechanism; site-directed mutagenesis and ESR spectroscopy showed that portal region residues undergo structural changes upon membrane interaction, with residues pointing outward decreasing in mobility and inner residues increasing in mobility to facilitate FA delivery.\",\n      \"method\": \"Site-directed mutagenesis, electron spin resonance (ESR) spectroscopy with spin-labeled protein mutants and lipid probes, lipidic micelle model membranes\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — reconstituted in vitro system with mutagenesis and biophysical spectroscopy; direct structural-mechanistic insight\",\n      \"pmids\": [\"23555925\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"FABP7 and FABP5 are differentially expressed in oligodendrocyte lineage cells: FABP7 is expressed in NG2+/PDGFRα+ oligodendrocyte progenitor cells (OPCs) while FABP5 marks mature oligodendrocytes; FABP7-KO OPCs show decreased proliferation and reduced differentiation into O4+ oligodendrocytes.\",\n      \"method\": \"Immunofluorescence co-staining with lineage markers in vivo and in vitro, BrdU proliferation assay, FABP7-KO and FABP5-KO OPC cultures, oligodendrocyte differentiation medium\",\n      \"journal\": \"Cell and tissue research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — KO with defined cellular phenotypes, replicated in vivo and in vitro with multiple markers\",\n      \"pmids\": [\"24114376\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"REV-ERBα (Nr1d1) directly represses Fabp7 gene expression in the brain; loss of Rev-erbα results in Fabp7 overexpression in multiple brain areas including the hippocampal subgranular zone, leading to increased proliferation of hippocampal neuronal progenitors and loss of diurnal proliferation patterns.\",\n      \"method\": \"Rev-erbα KO mouse gene expression comparison, in vitro cell proliferation and migration assays with Fabp7 manipulation and REV-ERBα activity modulation\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — KO with defined neurogenic phenotype; single lab\",\n      \"pmids\": [\"24932636\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"A distinct chimeric FABP7 isoform (LTR2-FABP7) is ectopically expressed in a subset of diffuse large B-cell lymphoma through activation of an endogenous retroviral LTR2 promoter; this isoform is required for DLBCL cell line proliferation and growth.\",\n      \"method\": \"Whole transcriptome reanalysis, RT-PCR confirmation in DLBCL cell lines, in vitro siRNA knockdown with proliferation readout\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vitro loss-of-function with proliferation readout; single lab\",\n      \"pmids\": [\"25114248\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Astrocyte-expressed FABP7 regulates dendritic morphology and excitatory synaptic function of cortical neurons; FABP7 KO astrocytes cause aberrant dendritic morphology, decreased spine density, reduced excitatory synapse number, and decreased mEPSC amplitude and frequency in mPFC pyramidal neurons; transplantation of WT astrocytes into the mPFC of KO mice partially rescued behavioral impairments.\",\n      \"method\": \"Fabp7 KO mice, Golgi staining, primary co-culture of neurons with KO astrocytes, conditioned medium experiments, whole-cell voltage-clamp recording (mEPSC), astrocyte transplantation\",\n      \"journal\": \"Glia\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — multiple orthogonal methods (electrophysiology, morphology, co-culture, transplantation rescue) establishing astrocytic FABP7 as regulator of neuronal synaptic function\",\n      \"pmids\": [\"26296243\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"DHA stimulates FABP7 expression in astrocytes via a PI3K/AKT-PPARγ axis; FABP7 then interacts physically with PPARγ (detected as protein-protein complex), displacing CDK5-PPARγ complex and leading to increased GFAP expression; FABP7 silencing suppresses DHA-induced GFAP upregulation.\",\n      \"method\": \"Primary rat brain astrocyte cultures, siRNA knockdown, PI3K/AKT and PPARγ inhibitor treatments, co-immunoprecipitation (FABP7-PPARγ and CDK5-PPARγ complexes), PPARγ-responsive element reporter assay\",\n      \"journal\": \"Journal of neurochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — co-IP of FABP7-PPARγ interaction plus siRNA phenotype; single lab\",\n      \"pmids\": [\"27787894\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"FABP7 (Fabp7) is required for normal sleep across phylogenetically disparate species; the FABP7.T61M missense mutation is associated with fragmented sleep in humans and recapitulated in mice and Drosophila; transgenic flies expressing FABP7.T61M in astrocytes show fragmented sleep, establishing FABP7 as part of a conserved astrocytic lipid-signaling pathway regulating sleep.\",\n      \"method\": \"Human sleep phenotyping (missense mutation association), Fabp7-deficient mice sleep analysis (EEG/EMG), Drosophila transgenic lines expressing FABP7.T61M in glia (sleep monitoring)\",\n      \"journal\": \"Science advances\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — conserved across three species with specific missense mutation; multiple independent model systems establish causal role\",\n      \"pmids\": [\"28435883\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"FABP7 can be regulated by PKC and the MAPK/ERK1/2 pathway in melanoma cells (PMA or MEK1 inhibitor downregulates FABP7); siRNA knockdown of FABP7 decreases melanoma cell proliferation and invasion without affecting apoptosis.\",\n      \"method\": \"PMA and MEK1 inhibitor (PD98059) treatment, siRNA knockdown, proliferation and invasion assays in human melanoma cell lines\",\n      \"journal\": \"BMC cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — pharmacological pathway manipulation plus siRNA with defined phenotype; single lab\",\n      \"pmids\": [\"18826602\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Glial FABP7 in hypothalamic astrocytes/tanycytes modulates neuronal leptin sensitivity; FABP7-KO mice show enhanced leptin-induced activation of ARC neurons (increased pSTAT3+ cells) and reduced weight gain on high-fat diet; primary FABP7-KO astrocytes display lower ERK phosphorylation after leptin treatment.\",\n      \"method\": \"FABP7 KO mice, diet-induced obesity model, leptin injection, immunohistochemistry (pSTAT3), primary astrocyte cultures with leptin treatment (ERK phosphorylation)\",\n      \"journal\": \"Molecular neurobiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vivo KO with defined neuroendocrine phenotype plus in vitro signaling; single lab\",\n      \"pmids\": [\"29623545\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"FABP7 drives metabolic reprogramming in HER2+ breast cancer brain metastasis by supporting a glycolytic phenotype and lipid droplet storage; FABP7 is required for upregulation of integrin-Src and VEGFA pathways and for in vivo tumor growth in the brain microenvironment.\",\n      \"method\": \"FABP7 knockdown and overexpression in HER2+ breast cancer cells, in vitro metabolic assays, in vivo intracranial xenograft model, pathway analysis\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — KO/OE with in vivo xenograft plus metabolic and pathway analysis; single lab\",\n      \"pmids\": [\"31324889\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"FABP7 protects astrocytes from ROS toxicity through lipid droplet (LD) formation; FABP7-KO astrocytes show significantly decreased LD accumulation, elevated ROS toxicity, impaired thioredoxin signaling, and activation of pro-apoptotic p38 MAPK and SAPK/JNK pathways; FABP7 overexpression in glioma cells increases LD accumulation and antioxidant enzyme expression.\",\n      \"method\": \"FABP7-KO primary mouse astrocytes, ROS induction, LD quantification, Western blot (TRX, PRX1, p38 MAPK, SAPK/JNK, caspase-3), NAC rescue, FABP7 overexpression in U87 cells\",\n      \"journal\": \"Molecular neurobiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — KO and OE with multiple orthogonal readouts (LD, ROS, signaling, apoptosis, rescue); mechanistically defined\",\n      \"pmids\": [\"30680690\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"FABP7 overexpression in astrocytes induces an NF-κB-driven pro-inflammatory response that is detrimental for motor neuron survival; silencing FABP7 in astrocytes from symptomatic hSOD1-expressing mice decreases inflammatory markers and reduces toxicity toward co-cultured motor neurons; a ligand-binding impaired mutant FABP7 does not induce NF-κB activation.\",\n      \"method\": \"FABP7 overexpression in non-transgenic astrocytes, astrocyte-motor neuron co-culture, siRNA knockdown, NF-κB reporter assay, hSOD1 transgenic mouse astrocyte cultures, mutant FABP7 (ligand-binding impaired)\",\n      \"journal\": \"Glia\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — gain and loss-of-function with mechanistic NF-κB pathway placement and mutant FABP7 control; multiple orthogonal methods\",\n      \"pmids\": [\"32619303\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"FABP7 interacts with ATP-citrate lyase (ACLY) in the nucleus and is important for acetyl-CoA metabolism; the FABP7-ACLY interaction modulates nuclear histone acetylation and thereby epigenetically regulates caveolin-1 expression in astrocytes and glioma cells.\",\n      \"method\": \"Co-immunoprecipitation (FABP7-ACLY interaction), FABP7-KO primary astrocytes, NIH-3T3 gain-of-function model, histone acetylation assay, caveolin-1 promoter analysis\",\n      \"journal\": \"Molecular neurobiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — co-IP identifying ACLY as binding partner, KO and OE with epigenetic readout; multiple orthogonal methods\",\n      \"pmids\": [\"32812201\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"FABP7 is required for optimal OPC differentiation during developmental myelination but is dispensable for remyelination; Fabp7 knockdown reduces OPC differentiation in vitro and Fabp7 KO mice show a transient delay in developmental myelination that resolves before adulthood.\",\n      \"method\": \"Fabp7 siRNA knockdown in OPC cultures, Fabp7 KO mouse developmental myelination analysis, focal demyelination model (remyelination assay)\",\n      \"journal\": \"Glia\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vitro KD and in vivo KO with specific myelination phenotype; single lab\",\n      \"pmids\": [\"32017258\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Rev-erbα directly binds the Fabp7 promoter in multiple brain areas (hippocampus, hypothalamus, VTA) as shown by ChIP-seq, and Fabp7 gene expression is specifically and robustly upregulated (>6-fold across all brain regions) in Rev-erbα KO mice, establishing Rev-erbα as a direct transcriptional repressor of Fabp7.\",\n      \"method\": \"ChIP-seq (Rev-erbα binding at Fabp7 promoter), Rev-erbα KO mouse, quantitative mRNA analysis across multiple brain areas\",\n      \"journal\": \"Current research in neurobiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — ChIP-seq direct binding evidence plus in vivo KO; mechanistically defined\",\n      \"pmids\": [\"34056625\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Ligand-bound FABP7 drives melanoma cell proliferation via activation of Wnt/β-catenin signaling; wild-type FABP7 overexpression increases Wnt/β-catenin activity (luciferase reporter), cyclin D1 expression, and proliferation, while a FA-binding site mutant FABP7 abrogates these effects; pharmacological inhibition of FABP7 with MF6 suppresses these responses.\",\n      \"method\": \"FABP7 siRNA knockdown and OE with wild-type vs. mutant FABP7, Wnt/β-catenin luciferase reporter assay, proliferation and migration assay, MF6 pharmacological inhibition\",\n      \"journal\": \"Pharmaceutical research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — reporter assay, ligand-binding mutant control, pharmacological inhibition; multiple orthogonal methods establishing ligand-binding dependence\",\n      \"pmids\": [\"33646504\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"FABP7 facilitates uptake of DHA in GBM neural stem-like cells; FABP7 knockdown reduces DHA incorporation into GBM cells and diminishes DHA-induced inhibition of cell migration.\",\n      \"method\": \"FABP7 knockdown in patient-derived GBM neurosphere cultures, fatty acid composition analysis (lipidomics), migration assay\",\n      \"journal\": \"Nutrients\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — KD with specific FA uptake and functional migration readout; single lab\",\n      \"pmids\": [\"34444824\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Nuclear FABP7 promotes glioblastoma cell proliferation in IDH1-wild-type glioma through caveolae formation; FABP7wt overexpression increases caveolin-1 expression and caveolae/caveosome formation via elevated H3K27ac on the caveolin-1 promoter through ACLY-dependent nuclear acetyl-CoA regulation; mutant FABP7 (FA-binding impaired) abrogates these effects in vitro and in xenograft models.\",\n      \"method\": \"FABP7wt and FABP7mut overexpression in U87 cells, caveolae/caveosome visualization, H3K27ac ChIP on caveolin-1 promoter, nuclear acetyl-CoA measurement, in vivo xenograft, patient GBM tissue analysis\",\n      \"journal\": \"Molecular oncology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — ChIP, mutant control, in vivo xenograft, nuclear acetyl-CoA measurement; multiple orthogonal methods\",\n      \"pmids\": [\"34716958\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"NMR and molecular dynamics simulations demonstrate that FABP7 has high conformational heterogeneity that is substantially reduced upon fatty acid ligand binding; DHA binding leads to chemical shift perturbations in residues near the nuclear localization signal, suggesting a mechanism for differential nuclear vs. cytoplasmic transport depending on ligand identity; ligand binding is resistant to mutations in polar binding pocket residues.\",\n      \"method\": \"NMR spectroscopy, multiscale molecular dynamics simulations, site-directed mutagenesis of binding pocket residues, biophysical binding assays\",\n      \"journal\": \"Biophysical journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — NMR plus MD simulations plus mutagenesis providing structural-mechanistic insight into ligand-directed transport\",\n      \"pmids\": [\"36698315\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Crystal structure of human FABP7 complexed with palmitic acid (a saturated FA) at 1.6 Å resolution reveals a U-shaped binding conformation; the carboxylate of palmitic acid interacts with Tyr129, Arg127, and via water bridge with Arg107 and Thr54, while the aliphatic chain is stabilized by hydrophobic interactions with Met21, Leu24, Thr30, Thr37, Pro39, Phe58, and Asp77; PA, OA, and DHA adopt distinct binding conformations in the pocket.\",\n      \"method\": \"X-ray crystallography (1.6 Å resolution), structural comparison with OA- and DHA-bound FABP7 and other FABP family members\",\n      \"journal\": \"Acta crystallographica. Section D, Structural biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — crystal structure with detailed binding interactions characterized at atomic resolution\",\n      \"pmids\": [\"34196621\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Oleic acid-bound FABP7 drives glioma cell proliferation by promoting nuclear localization of the FABP7-OA complex, inducing nuclear lipid droplet (nLD) formation, increasing colocalization of nLD with PML nuclear bodies, and enhancing histone acetylation-dependent transcription of proliferation-related genes; FA-binding site mutant FABP7 abrogates all these effects.\",\n      \"method\": \"OA treatment of FABP7-expressing cells, FABP7 nuclear localization imaging, nLD visualization, PML body co-localization, histone acetylation assay, mRNA profiling, FABP7-KO and FABP7-mutant overexpression controls\",\n      \"journal\": \"The FEBS journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — mechanistic chain from ligand binding to nuclear LD formation to histone acetylation to gene expression, with mutant FABP7 control; multiple orthogonal methods\",\n      \"pmids\": [\"36325660\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"FABP7 promotes NSCLC metastasis by competitively inhibiting the interaction between β-catenin and its cytoplasmic degradation complex, thereby repressing phosphorylation-dependent ubiquitination and degradation of β-catenin and activating canonical Wnt signaling.\",\n      \"method\": \"FABP7 KD and OE in NSCLC cell lines, in vivo metastasis model, co-immunoprecipitation (β-catenin with degradation complex), β-catenin phosphorylation and ubiquitination assays\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — co-IP showing FABP7 competition with β-catenin degradation complex; single lab\",\n      \"pmids\": [\"35269427\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Wild-type FABP7 overexpression induces an NF-κB-driven inflammatory response in human iPSC-derived astrocytes (identified by RNA-seq as top biological process); a ligand-binding impaired mutant FABP7 does not activate NF-κB, demonstrating that FABP7's pro-inflammatory function requires its fatty acid-binding activity; amyloid-β treatment induces FABP7 upregulation in primary hippocampal astrocytes.\",\n      \"method\": \"FABP7 OE in human iPSC-derived astrocytes, whole transcriptome RNA-seq, Gene Ontology analysis, NF-κB reporter assay, ligand-binding mutant FABP7 control, Aβ treatment of primary astrocytes, APP/PS1 mouse immunostaining\",\n      \"journal\": \"GeroScience\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — RNA-seq with OE/mutant comparison, NF-κB reporter, and ligand-binding mutant control; multiple orthogonal methods\",\n      \"pmids\": [\"37688656\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"FABP7 forms hetero-aggregates with α-synuclein (αSyn) that exhibit stronger toxicity than αSyn aggregates alone; injected FABP7/αSyn hetero-aggregates selectively accumulate in oligodendrocytes and Purkinje neurons causing cerebellar dysfunction; epsin-2 regulates FABP7/αSyn hetero-aggregate propagation via clathrin-dependent endocytosis, and epsin-2 knockdown decreases αSyn aggregate accumulation and improves motor performance.\",\n      \"method\": \"MSA mouse models (PLP-hαSyn, FABP7/αSyn hetero-aggregate injection), co-aggregation assays, AAV5-dependent epsin-2 knockdown, histology, motor function testing, bioinformatic analysis of MSA patient whole blood\",\n      \"journal\": \"Brain : a journal of neurology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — direct in vivo hetero-aggregate injection, cell-type selective accumulation, and epsin-2 epistasis with rescue; multiple methods\",\n      \"pmids\": [\"37082980\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"FABP7 binds oleic acid and DHA micelles through its portal region residues; NMR and molecular dynamics simulations reveal that binding to micelles occurs through the same portal region as membrane binding, and simulations capture fatty acid dissociation from membranes directly entering FABP7's binding pocket.\",\n      \"method\": \"NMR spectroscopy, multiscale molecular dynamics simulations, biophysical binding assays with OA and DHA micelles\",\n      \"journal\": \"Biophysical journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — direct NMR plus MD simulations capturing atomic-level binding mechanism; multiple complementary biophysical methods\",\n      \"pmids\": [\"36698315\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"FABP7 deficiency in iPSC-derived cerebral organoids from normocephalic ASD individuals causes premature neural differentiation of neural stem cells; altered phosphorylation of MEK1/2 (downstream of FABP7) was detected, and regulation of the FABP7/MEK pathway reversed improper neural differentiation; Fabp7 knockdown and MEK2-overexpressing mice exhibit repetitive stereotyped behaviors and social defects.\",\n      \"method\": \"iPSC-derived cerebral organoids from ASD patients, single-cell RNA-seq (time series), FABP7 loss-of-function rescue experiments via FABP7/MEK pathway modulation, Fabp7 KD mice behavioral phenotyping (open field, social interaction)\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — human organoid model + pathway rescue + in vivo KD mouse phenotype; multiple orthogonal methods across human and mouse\",\n      \"pmids\": [\"39556706\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"FABP7 in hepatic macrophages modulates M2 polarization via PPARγ and its target genes (CCL17, TGF-β); FABP7-deficient macrophages display decreased PPARγ activity, reduced fibrotic response of myofibroblasts, and decreased CD4+ T-cell migration into liver; in vitro, IL-4-stimulated FABP7-deficient macrophages show reduced CCL-17 and TGF-β, effects blocked by PPARγ inhibitor.\",\n      \"method\": \"FABP7 KO in CCl4-induced hepatic fibrosis model, in vitro macrophage polarization assays, PPARγ inhibitor treatment, co-culture of macrophages with CD4+ T cells and hepatic stellate cells\",\n      \"journal\": \"Journal of immunology research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — KO in vivo model plus in vitro mechanistic validation with PPARγ inhibitor; single lab\",\n      \"pmids\": [\"40017805\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Extracellular FABP7 induces a pro-inflammatory phenotype in monocytes via increased glycolysis, upregulating CD16, CD80 and IL-1β; FABP7-induced gene expression in monocytes reflects enhanced inflammation, chemotaxis, and glucose metabolism.\",\n      \"method\": \"In vitro FABP7 treatment of monocytes, flow cytometry (CD16, CD80), ELISA (IL-1β), transcriptomics, glycolysis assays; patient serum/CSF FABP7 measurement\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vitro mechanistic experiment with multiple readouts establishing glycolytic switch; single lab but published in high-impact journal\",\n      \"pmids\": [\"40595541\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"FABP7 silencing in astrocytes decreases NF-κB-p65 nuclear translocation and NF-κB reporter activity in response to multiple inflammatory stimuli, reduces astrocyte toxicity toward motor neurons, and reduces glial activation in vivo after LPS administration; whole transcriptome RNA-seq confirms attenuation of NF-κB-dependent transcriptional response.\",\n      \"method\": \"FABP7 siRNA in primary mouse and human iPSC-derived astrocytes, NF-κB reporter assay, NF-κB-p65 nuclear translocation imaging, astrocyte-motor neuron co-culture, in vivo astrocytic FABP7 knockdown in LPS-treated mice, RNA-seq\",\n      \"journal\": \"Glia\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple cell types (mouse, human iPSC-derived), in vivo validation, RNA-seq; mechanistically placed in NF-κB pathway\",\n      \"pmids\": [\"40251832\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"YRDC-catalyzed tRNA t6A modification drives codon-biased translation of FABP7 mRNA; elevated FABP7 induces lipid droplet accumulation that sequesters TMZ-induced ROS to confer chemoresistance in glioblastoma; YRDC inhibition suppresses FABP7 translation and lipid droplets, synergizing with TMZ in vitro and in orthotopic xenografts.\",\n      \"method\": \"YRDC KD/OE, polysome profiling/ribosome profiling (codon-biased translation), lipid droplet quantification, ROS assays, in vitro and in vivo (PDX) TMZ resistance models, YRDC inhibitor (HY-Q66655) virtual screening and functional validation\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — mechanistic chain from tRNA modification to FABP7 translation to LD to chemoresistance; single lab but multiple orthogonal methods\",\n      \"pmids\": [\"42014887\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"FABP7 is an astrocyte/radial glia-enriched intracellular lipid chaperone that binds long-chain polyunsaturated fatty acids (especially DHA and arachidonic acid) through a defined binding pocket and delivers them via a portal-region-mediated collisional mechanism to membranes or to the nucleus, where ligand identity dictates subcellular trafficking; in the nucleus FABP7 interacts with ACLY to regulate acetyl-CoA levels and histone acetylation, epigenetically controlling genes such as caveolin-1, and activates NF-κB-driven inflammatory responses in a ligand-binding-dependent manner; at the cellular level FABP7 maintains neural stem/progenitor cell proliferation downstream of Pax6, regulates astrocyte-dependent dendritic morphology and excitatory synaptic function, modulates sleep across species through astrocytic lipid signaling, promotes lipid droplet formation to protect against ROS, and in cancer contexts drives proliferation and invasion through Wnt/β-catenin, MEK/ERK, and glycolytic reprogramming pathways.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"FABP7 is an intracellular fatty acid-binding protein that functions as a lipid chaperone in radial glia, astrocytes, and neural stem/progenitor cells, coupling fatty acid transport to nuclear signaling, epigenetic regulation, and inflammatory responses. FABP7 binds long-chain polyunsaturated fatty acids (DHA, oleic acid, arachidonic acid) in a β-barrel pocket and delivers them to membranes via a portal-region-mediated collisional mechanism; ligand identity dictates conformational changes near the nuclear localization signal, directing subcellular trafficking of the FABP7–fatty acid complex to the nucleus where it interacts with ACLY to regulate acetyl-CoA levels and histone acetylation at targets including caveolin-1 [PMID:23555925, PMID:36698315, PMID:34196621, PMID:32812201, PMID:36325660]. In development, FABP7 acts downstream of Pax6 and is repressed by REV-ERBα, maintaining neural stem cell proliferation and regulating oligodendrocyte progenitor differentiation; its loss causes premature neuronal differentiation, disrupted dendritic morphology, and reduced excitatory synaptic function through astrocyte-dependent mechanisms [PMID:16237179, PMID:34056625, PMID:26296243, PMID:22581784]. FABP7 activates NF-κB-driven neuroinflammation in a ligand-binding-dependent manner, promotes lipid droplet formation that sequesters reactive oxygen species, and regulates sleep through a conserved astrocytic lipid-signaling pathway disrupted by the human T61M missense variant [PMID:40251832, PMID:32619303, PMID:30680690, PMID:28435883].\",\n  \"teleology\": [\n    {\n      \"year\": 1994,\n      \"claim\": \"The discovery that FABP7 (BLBP) is a brain-specific lipid-binding protein localizing to both nucleus and cytoplasm of radial glia, and that its antibody-mediated blockade disrupts the radial glial fiber system, established FABP7 as a functional mediator of glial differentiation rather than a passive lipid carrier.\",\n      \"evidence\": \"Immunoelectron microscopy for subcellular localization, anti-BLBP antibody blockade in primary brain cell cultures\",\n      \"pmids\": [\"8161459\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Identity of the endogenous lipid ligand was unknown\", \"Mechanism linking lipid binding to radial glial fiber formation was not defined\", \"Nuclear function was not explored\"]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Placing FABP7 downstream of Pax6 and showing that its knockdown causes premature neuronal differentiation established FABP7 as a transcriptionally regulated effector maintaining neural stem/progenitor cell proliferation.\",\n      \"evidence\": \"In vivo electroporation of siRNA in embryonic rat cortex with BrdU proliferation assay; Pax6 overexpression inducing Fabp7\",\n      \"pmids\": [\"16237179\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether FABP7 is a direct versus indirect Pax6 target was not resolved at this stage\", \"Downstream lipid-dependent effectors of proliferation maintenance were unknown\"]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"Fabp7 knockout mice exhibiting decreased prepulse inhibition and disrupted neurogenesis linked FABP7 to NMDA receptor-related circuits and sensorimotor gating, broadening its role from development to postnatal brain function.\",\n      \"evidence\": \"QTL analysis, Fabp7 KO mouse behavioral phenotyping, BrdU neurogenesis assay, quantitative complementation\",\n      \"pmids\": [\"18001149\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether the PPI deficit is cell-autonomous to glia or neurons was unclear\", \"Molecular pathway from FABP7 to NMDA receptor signaling was not defined\"]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"The observation that Fabp7 mRNA and protein undergo diurnal oscillations in adult astrocytes, peaking at opposite phases, suggested post-transcriptional regulation and a role in circadian brain physiology.\",\n      \"evidence\": \"RNA and protein time-course analysis across 24 h in adult mouse brain by in situ hybridization and immunoblot\",\n      \"pmids\": [\"18286188\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Transcriptional versus post-transcriptional basis of oscillation was not resolved\", \"Functional consequence of diurnal FABP7 cycling was not tested\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Multiple studies converged to show that FABP7 mRNA undergoes CPEB1-dependent polyadenylation for perisynaptic localization in astrocytes, that PAX6 directly transactivates the FABP7 promoter, and that FABP7 maintains neural stem cell proliferation in the adult hippocampus, integrating transcriptional, post-transcriptional, and stem cell biology dimensions.\",\n      \"evidence\": \"Co-IP of Fabp7 mRNA with CPEB1, Xenopus CPE reporter assay, PAX6 promoter deletion/gel shift, Fabp7 KO hippocampal BrdU assays\",\n      \"pmids\": [\"22279223\", \"22583899\", \"22581784\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether CPEB1-dependent translation directly regulates perisynaptic lipid metabolism was not shown\", \"Full set of transcription factors controlling FABP7 expression was incomplete\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Biophysical and structural studies demonstrated that FABP7 delivers fatty acids to membranes via a portal-region collisional mechanism, with helices αI/αII undergoing conformational rearrangement, providing the first mechanistic model for FABP7-mediated lipid transfer.\",\n      \"evidence\": \"Site-directed mutagenesis, ESR spectroscopy with spin-labeled mutants and lipid probes\",\n      \"pmids\": [\"23555925\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether the collisional mechanism operates identically at nuclear versus plasma membranes was untested\", \"Kinetic parameters of transfer for different FA species were not measured\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"ChIP and KO data established REV-ERBα as a direct transcriptional repressor of Fabp7 in the brain, connecting clock machinery to FABP7-driven progenitor proliferation and providing a molecular link between circadian regulation and neurogenesis.\",\n      \"evidence\": \"Rev-erbα KO mouse, promoter ChIP-seq, cell proliferation assays\",\n      \"pmids\": [\"24932636\", \"34056625\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether REV-ERBα repression accounts for the full diurnal FABP7 oscillation was not resolved\", \"Other circadian regulators of FABP7 were not excluded\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Demonstrating that FABP7-KO astrocytes impair dendritic morphology, spine density, and excitatory synaptic transmission of co-cultured neurons — with partial rescue by WT astrocyte transplantation — established FABP7 as an astrocytic regulator of neuronal circuit structure and function.\",\n      \"evidence\": \"Fabp7 KO mice, Golgi staining, neuron-astrocyte co-culture, mEPSC recording, astrocyte transplantation in mPFC\",\n      \"pmids\": [\"26296243\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The secreted or contact-dependent astrocytic signal was not identified\", \"Whether specific FABP7-transported lipids mediate the synaptic effects was unknown\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The T61M missense variant's association with fragmented sleep in humans, mice, and Drosophila — with astrocyte-specific expression in flies — established FABP7 as part of a phylogenetically conserved astrocytic lipid-signaling pathway regulating sleep.\",\n      \"evidence\": \"Human genotype-phenotype association, Fabp7 KO mouse EEG/EMG, transgenic Drosophila expressing FABP7.T61M in glia\",\n      \"pmids\": [\"28435883\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Downstream lipid signals mediating sleep consolidation were not identified\", \"Whether the T61M mutation alters ligand binding specificity or affinity was not structurally resolved\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"FABP7 was shown to promote lipid droplet formation that protects astrocytes from ROS toxicity via thioredoxin signaling, and to support glycolytic reprogramming in HER2+ breast cancer brain metastasis, linking its lipid-shuttling function to metabolic stress responses.\",\n      \"evidence\": \"FABP7 KO astrocytes with ROS induction and LD quantification; FABP7 KD/OE in HER2+ cells with metabolic assays and intracranial xenograft\",\n      \"pmids\": [\"30680690\", \"31324889\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether LD-mediated ROS protection requires specific FA species was untested\", \"Direct lipid cargo in cancer metabolic reprogramming was not identified\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Discovery that FABP7 interacts with ACLY in the nucleus and modulates histone acetylation (including H3K27ac at the caveolin-1 promoter) revealed an epigenetic effector function, while ligand-binding-dependent NF-κB activation in astrocytes linked FABP7 to neuroinflammation in ALS models.\",\n      \"evidence\": \"Co-IP of FABP7–ACLY, histone acetylation ChIP, FABP7 OE/KO in astrocytes, NF-κB reporter, ligand-binding mutant control, hSOD1 astrocyte co-culture\",\n      \"pmids\": [\"32812201\", \"32619303\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether ACLY interaction requires a specific lipid ligand was not resolved\", \"Structural basis of FABP7–ACLY interaction was unknown\", \"Whether NF-κB activation is direct or mediated through ACLY/acetyl-CoA was not distinguished\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Crystal structures of FABP7 with different fatty acids and NMR/MD studies showing ligand-dependent conformational changes near the NLS provided a structural explanation for how lipid identity directs FABP7's nuclear versus cytoplasmic distribution, and ligand-bound FABP7 was shown to activate Wnt/β-catenin signaling in melanoma.\",\n      \"evidence\": \"X-ray crystallography at 1.6 Å, NMR spectroscopy, MD simulations, mutagenesis; Wnt/β-catenin reporter with WT vs. FA-binding-site mutant FABP7, MF6 pharmacological inhibition\",\n      \"pmids\": [\"34196621\", \"36698315\", \"33646504\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis for NLS exposure upon specific ligand binding remains at simulation level\", \"Whether Wnt activation is direct or through β-catenin degradation complex competition was not fully resolved at this point\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Oleic acid-bound FABP7 was shown to drive nuclear lipid droplet formation colocalizing with PML bodies and enhancing histone acetylation-dependent proliferative gene expression, providing a complete mechanistic chain from ligand binding through nuclear LD to epigenetic transcriptional control.\",\n      \"evidence\": \"FABP7 OE with OA, nuclear LD and PML body colocalization imaging, histone acetylation assay, mRNA profiling, FABP7 FA-binding mutant control\",\n      \"pmids\": [\"36325660\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether nuclear LD formation requires ACLY-dependent acetyl-CoA was not directly tested in this study\", \"PML body functional requirement was not confirmed by PML loss-of-function\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"FABP7's pro-inflammatory NF-κB activation was validated in human iPSC-derived astrocytes with RNA-seq and shown to require fatty acid binding, while FABP7 was also found to form toxic hetero-aggregates with α-synuclein that accumulate in oligodendrocytes via epsin-2-dependent endocytosis, extending FABP7's pathological roles to Alzheimer's and multiple system atrophy.\",\n      \"evidence\": \"FABP7 OE in iPSC astrocytes with RNA-seq and ligand-binding mutant; FABP7/αSyn hetero-aggregate injection in MSA mouse models, AAV5-epsin-2 KD rescue\",\n      \"pmids\": [\"37688656\", \"37082980\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Which specific FA species drive NF-κB activation in human astrocytes was not determined\", \"Whether FABP7/αSyn aggregation is relevant in sporadic Parkinson's disease was not tested\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"FABP7 deficiency in ASD patient-derived cerebral organoids caused premature neural differentiation rescued by MEK pathway modulation, and Fabp7-KD mice exhibited ASD-like behaviors, establishing FABP7/MEK as a functional axis in autism-relevant neural development.\",\n      \"evidence\": \"iPSC-derived cerebral organoids, scRNA-seq time series, FABP7/MEK pathway rescue, Fabp7 KD mouse behavioral phenotyping\",\n      \"pmids\": [\"39556706\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether FABP7 directly activates MEK or acts through an intermediate lipid signal was not resolved\", \"Genetic variants in FABP7 causative for ASD in families were not identified\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extracellular FABP7 was shown to reprogram monocyte metabolism toward glycolysis and inflammation, while intracellular FABP7 in hepatic macrophages modulates PPARγ-dependent M2 polarization, and astrocytic FABP7 silencing attenuates NF-κB-p65 nuclear translocation in vivo, consolidating FABP7 as a lipid-dependent inflammatory mediator across cell types.\",\n      \"evidence\": \"In vitro monocyte treatment with extracellular FABP7, FABP7 KO in hepatic fibrosis model with PPARγ inhibitor, astrocytic FABP7 siRNA in vivo with LPS challenge and RNA-seq\",\n      \"pmids\": [\"40595541\", \"40017805\", \"40251832\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Receptor or uptake mechanism for extracellular FABP7 on monocytes is unknown\", \"Whether PPARγ and NF-κB pathways are independently or sequentially activated by FABP7 is unresolved\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Key unresolved questions include: the identity of specific lipid species that dictate FABP7's nuclear versus cytoplasmic function in vivo; the structural basis of the FABP7–ACLY interaction; the receptor or mechanism for extracellular FABP7 uptake; and whether FABP7-dependent sleep regulation operates through the same NF-κB/epigenetic axis identified in neuroinflammation.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural model of FABP7–ACLY complex exists\", \"Lipid species specificity for each downstream pathway is undefined in vivo\", \"Mechanism linking FABP7 to sleep at the molecular level is uncharacterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008289\", \"supporting_discovery_ids\": [0, 10, 28, 29, 34]},\n      {\"term_id\": \"GO:0140104\", \"supporting_discovery_ids\": [10, 34]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [21, 22, 25, 31, 32, 38]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 22, 27, 28, 30]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 8]},\n      {\"term_id\": \"GO:0005811\", \"supporting_discovery_ids\": [20, 30, 39]},\n      {\"term_id\": \"GO:0005576\", \"supporting_discovery_ids\": [37]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [1, 9, 22, 27, 30]},\n      {\"term_id\": \"R-HSA-4839726\", \"supporting_discovery_ids\": [22, 27, 30]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [15, 21, 25, 31, 32, 38]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [0, 1, 6, 11, 35]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [21, 32, 36, 37, 38]},\n      {\"term_id\": \"R-HSA-1430728\", \"supporting_discovery_ids\": [19, 20, 26, 39]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"ACLY\",\n      \"CPEB1\",\n      \"PPARG\",\n      \"PAX6\",\n      \"NR1D1\",\n      \"SNCA\",\n      \"CTNNB1\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}