Affinage

SLC27A2

Long-chain fatty acid transport protein 2 · UniProt O14975

Length
620 aa
Mass
70.3 kDa
Annotated
2026-06-10
37 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/7 claims corpus-supported (86%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SLC27A2/FATP2 is a localization-dependent, bifunctional protein that couples cellular long-chain fatty acid (LCFA) uptake to fatty acid activation, governing tissue lipid metabolism and lipid-driven pathology (PMID:20530735, PMID:24113382). Its two enzymatic activities are mechanistically separable: a transport function that drives LCFA uptake and an intrinsic very long-chain acyl-CoA synthetase activity that directly generates C20:4-CoA and C22:6-CoA, while partnering with long-chain acyl-CoA synthetases (ACSLs) to esterify shorter chains through vectorial acylation (PMID:20530735, PMID:24113382, PMID:37172427). This dissociability is established by a naturally occurring splice variant (FATP2b) that retains transport but lacks synthetase activity and by small molecules (Lipofermata, Grassofermata) that block transport without affecting synthetase activity (PMID:19913517, PMID:27446528). FATP2 abundance and membrane positioning are tightly regulated: NRF2 directly transactivates FATP2 to enhance fatty acid uptake and drive hepatic steatosis (PMID:40303331), and loss of the epoxygenase Cyp2c44 increases plasma membrane FATP2, promoting DAG accumulation, PKCδ activation, IRS-1 serine phosphorylation, and insulin resistance (PMID:38743615). Through apical NEFA uptake in kidney proximal tubule epithelium, FATP2 mediates palmitate-induced lipoapoptosis and proteinuria-induced tubular injury (PMID:28993506). FATP2-dependent fatty acid uptake also fuels disease-relevant programs in other tissues: it supports melanoma resistance to BRAF/MEK inhibition via mitochondrial metabolism (PMID:32499221), drives arachidonic-acid-triggered NLRP3 inflammasome activation in myeloid-derived suppressor cells (PMID:37916155), and promotes osteoclastogenesis through β-oxidation and ROS (PMID:38477781). In pancreatic α-cells FATP2 inhibition increases GLP-1 secretion that paracrine-stimulates β-cell insulin release (PMID:39975070).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2009 Medium

    Established that FATP2-mediated fatty acid transport could be pharmacologically separated from acyl-CoA synthetase activity, proving the two are distinct druggable functions.

    Evidence High-throughput screen in yeast expressing human FATP2 with follow-up uptake and synthetase assays in human cell lines

    PMID:19913517

    Open questions at the time
    • Did not define the structural basis of transport vs. synthetase activity
    • Selectivity of inhibitors across other FATP family members not resolved
  2. 2010 High

    Resolved the long-standing ambiguity over FATP2's primary in vivo role by showing it acts mainly as a plasma membrane LCFA transporter rather than a peroxisomal VLACS enzyme in liver.

    Evidence Liver-specific AAV8 shRNA knockdown with subcellular fractionation, VLACS activity, and radiolabeled uptake assays in mice

    PMID:20530735

    Open questions at the time
    • Did not establish how transport is mechanistically coupled to esterification
    • Peroxisomal contribution in other tissues unaddressed
  3. 2011 Medium

    Showed FATP2 can localize to the ER in human hepatoma cells and drives uptake indirectly through esterification, framing the vectorial acylation model.

    Evidence Immunofluorescence co-localization, overexpression, ACS activity and oleic acid/BODIPY-C12 uptake assays in HuH7/HepG2

    PMID:22022213

    Open questions at the time
    • Localization conflicts with plasma-membrane role seen in liver—context dependence not reconciled
    • No independent replication reported
  4. 2013 Medium

    Defined the dual biochemical logic: FATP2 partners with ACSLs for LCFA-CoA generation while intrinsically activating very long-chain species, and reshapes fatty acid trafficking into specific phospholipid classes.

    Evidence Stable-isotope fatty acid tracing with MS-based lipidomics in overexpressing cells

    PMID:24113382

    Open questions at the time
    • Direct physical ACSL partnership not demonstrated in this study
    • Species-selective trafficking mechanism unknown
  5. 2016 Medium

    Used an endogenous separation-of-function splice variant (FATP2b) to confirm transport and synthetase activities are genetically separable and validated transport-selective inhibitors in vivo.

    Evidence Splice variant characterization with enzymatic/uptake assays and in vitro/in vivo inhibitor studies in mice

    PMID:27446528

    Open questions at the time
    • Physiological regulation of FATP2b splicing not defined
    • Structural determinant of the lost synthetase activity unmapped
  6. 2017 High

    Identified FATP2 as the apical proximal tubule NEFA transporter whose uptake drives lipoapoptosis, linking it causally to tubular injury.

    Evidence Slc27a2 knockout mice, ex vivo microperfusion, shRNA knockdown, and proteinuria model with apoptosis readouts

    PMID:28993506

    Open questions at the time
    • Downstream apoptotic signaling from NEFA accumulation not detailed
    • Restriction of expression to proximal tubule mechanism unexplained
  7. 2020 Medium

    Connected FATP2-mediated lipid uptake to PPARα ligand provision and broad hepatic metabolic control, and to tumor lipid programming.

    Evidence Fatp2-/- mouse RNA-Seq and targeted metabolomics; melanoma co-culture, uptake, mitochondrial and in vivo therapy-resistance models

    PMID:32188695 PMID:32499221

    Open questions at the time
    • PPARα ligand link inferred from transcriptomics, not direct binding
    • Direct FATP2 substrate driving therapy resistance not isolated
  8. 2023 Medium

    Placed FATP2 upstream of innate immune and proliferative lipid programs—arachidonic-acid-driven NLRP3 activation in MDSCs and ACSL1-coupled lipid metabolism in cancer cells.

    Evidence Lipid uptake screening, in vivo ischemia-reperfusion/tumor recurrence model with Lipofermata; Co-IP and knockdown/overexpression in NSCLC cells

    PMID:37172427 PMID:37916155

    Open questions at the time
    • ACSL1 interaction rests on a single Co-IP without reciprocal validation
    • How arachidonic acid uptake mechanistically triggers mitochondrial ROS not fully resolved
  9. 2023 Low

    Provided a structural model of the FATP2 inhibitor binding site, enabling nanomolar inhibitor discovery.

    Evidence AlphaFold2-based homology model with site-directed mutagenesis, virtual screening, and uptake/apoptosis assays

    PMID:37307967

    Open questions at the time
    • Homology model, not an experimental structure
    • Limited mechanistic depth beyond mutagenesis validation
  10. 2023 High

    Identified the NRF2→FATP2 transcriptional axis as a driver of drug-induced hepatic steatosis, establishing direct transcriptional control of FATP2.

    Evidence ChIP and dual-luciferase reporter assays, NRF2 and FATP2 genetic mouse models, KEAP1 site-directed mutagenesis with VPA treatment

    PMID:40303331

    Open questions at the time
    • Other transcriptional regulators of FATP2 not surveyed
    • Tissue scope of NRF2 control beyond liver unknown
  11. 2024 Medium

    Defined post-translational and localization control of FATP2—USP29/CEACAM6-mediated stabilization and EET/Cyp2c44 control of plasma membrane localization feeding the DAG/PKCδ/IRS-1 insulin-resistance axis.

    Evidence Co-IP and deubiquitination assays with tumor models; Cyp2c44-/- mice with fractionation, lipidomics, PKCδ inhibition and EET-A rescue

    PMID:38743615 PMID:39562695

    Open questions at the time
    • CEACAM6/USP29 mechanism rests on Co-IP without reciprocal/structural validation
    • How EET signaling physically alters FATP2 trafficking is unknown
  12. 2024 Medium

    Extended FATP2's metabolic reach to osteoclastogenesis, where its fatty acid uptake fuels β-oxidation and ROS required for bone resorption.

    Evidence siRNA and Lipofermata inhibition, RNA-seq, and LPS-induced and ovariectomy bone-loss mouse models

    PMID:38477781

    Open questions at the time
    • Direct lipid substrate driving osteoclast energy metabolism not identified
    • Specificity for osteoclasts over osteoblasts mechanism unexplained
  13. 2025 Medium

    Revealed an α-cell-specific FATP2 role whose inhibition increases GLP-1 secretion and paracrine β-cell insulin release, defining a glucose-lowering axis.

    Evidence FATP2 KO (db/db), Lipofermata, GLP-1 receptor antagonist rescue, αTC1-6 and human islet assays (preprint)

    PMID:39975070

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • How loss of α-cell FATP2 lipid uptake triggers GLP-1 secretion mechanistically unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How FATP2 transport activity is mechanically coupled to acyl-CoA synthesis at the molecular level, and what determines its differential localization (plasma membrane vs. ER vs. peroxisome) across cell types, remains unresolved.
  • No experimental high-resolution structure of FATP2
  • Determinants of cell-type-specific localization not defined
  • Direct biochemical reconstitution of FATP2-ACSL vectorial acylation lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 5 GO:0008289 lipid binding 3 GO:0016874 ligase activity 3
Localization
GO:0005886 plasma membrane 3 GO:0005777 peroxisome 1 GO:0005783 endoplasmic reticulum 1
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-168256 Immune System 2 R-HSA-382551 Transport of small molecules 2
Partners
ACSL1CEACAM6USP29

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 FATP2 is a multifunctional protein with subcellular localization-dependent activity: in mouse liver, only a minor fraction localizes to peroxisomes where it contributes to ~50% of peroxisomal very long-chain acyl-CoA synthetase (VLACS) activity, while total hepatic VLACS activity is not significantly affected by FATP2 loss; in contrast, liver-specific FATP2 knockdown reduced long-chain fatty acid (LCFA) uptake by 40%, indicating that FATP2's primary hepatic role is as a plasma membrane-associated LCFA transporter rather than a peroxisomal enzyme. Liver-specific shRNA knockdown via AAV8, subcellular fractionation, VLACS activity assays, radiolabeled fatty acid uptake assays in mice American journal of physiology. Endocrinology and metabolism High 20530735
2011 In human hepatoma cells (HuH7, HepG2), FATP2 localizes to the endoplasmic reticulum (not plasma membrane); overexpression of FATP2 highly increases acyl-CoA synthetase activity and uptake of both radiolabeled oleic acid and fluorescent fatty acid analogue (BODIPY-C12), with FATP2 showing the highest effect on fatty acid uptake among the transporters tested, suggesting it drives uptake indirectly through esterification (vectorial acylation). Double immunofluorescence co-localization with ER markers, overexpression, ACS activity assay, [3H]-oleic acid uptake, FACS-based BODIPY-C12 uptake quantification International journal of medical sciences Medium 22022213
2013 FATP2 has dual function in fatty acid transport and activation: it can partner with long-chain acyl-CoA synthetases (ACSLs) to generate LCFA-CoAs (e.g., C16:0-CoA, C18:3-CoA) through vectorial acylation, while its intrinsic very long-chain acyl-CoA synthetase activity directly generates C20:4-CoA and C22:6-CoA; FATP2 expression also alters intracellular trafficking of exogenous fatty acids into phosphatidic acid and specific phospholipid classes (PC, PE, PI, PS) in a fatty acid species-selective manner. Stable isotopically labeled fatty acids (tracer), mass spectrometry-based lipidomics, overexpression in cells Biochemical and biophysical research communications Medium 24113382
2009 Human FATP2-mediated fatty acid transport can be selectively inhibited by small molecule compounds identified in a high-throughput screen using yeast expressing human FATP2; five representative compounds inhibited LCFA uptake with low-micromolar IC50 in FATP2-expressing Caco-2 and HepG2 cells but not in 3T3-L1 adipocytes (which lack FATP2), with no effect on long-chain acyl-CoA synthetase activity, glucose transport, or cell viability, demonstrating that fatty acid transport and activation can be pharmacologically dissociated. High-throughput screen in yeast expressing human FATP2, fluorescent fatty acid uptake assay (BODIPY-C12), IC50 determination in human cell lines, TEER, glucose transport assay, cell viability Biochemical pharmacology Medium 19913517
2016 A naturally occurring splice variant of FATP2, FATP2b (lacking exon 3), retains full fatty acid transport function but completely lacks acyl-CoA synthetase activity; use of this variant in inhibitor screens identified two compounds, Lipofermata and Grassofermata, as effective fatty acid transport inhibitors both in vitro and in vivo in mouse models, demonstrating that transport and synthetase activities are separable functions of FATP2. Splice variant characterization, enzymatic activity assays, fatty acid uptake assays, in vitro and in vivo inhibitor studies in mouse models MedChemComm Medium 27446528
2017 FATP2 (encoded by Slc27a2) is expressed exclusively in kidney proximal tubule epithelial cells along the apical but not basolateral membrane; Slc27a2 knockout mice are protected from proteinuria-induced tubular injury, and Slc27a2-null proximal tubules and FATP2 shRNA-treated proximal tubule cell lines show significantly reduced NEFA uptake and reduced palmitate-induced apoptosis, establishing FATP2 as a major apical proximal tubule NEFA transporter that mediates lipoapoptosis. Immunolocalization, mRNA/protein expression, Slc27a2 knockout mouse model, ex vivo microperfusion, in vitro shRNA knockdown, apoptosis assay, lipidated albumin-induced proteinuria model Journal of the American Society of Nephrology : JASN High 28993506
2020 In the aged tumor microenvironment, aged dermal fibroblasts secrete increased neutral lipids (especially ceramides); melanoma cells exposed to this lipid secretome upregulate FATP2, which mediates increased lipid uptake; FATP2-dependent lipid accumulation supports mitochondrial metabolism and drives resistance to BRAF/MEK inhibition, and FATP2 blockade overcomes this age-related resistance in animal models. Co-culture experiments, lipidomic analysis, FATP2 overexpression/knockdown, lipid uptake assays, mitochondrial metabolism assays, in vivo tumor models with targeted therapy Cancer discovery Medium 32499221
2020 Deletion of FATP2 in mouse liver shifts the transcriptomic landscape, upregulating PPARα-regulated genes involved in fatty acid degradation, peroxisome biogenesis, and fatty acid synthesis; targeted metabolomics shows increases in C16:0, C16:1, C18:1 fatty acids and lipid mediators (lipoxin A4, prostaglandin J2) and decreased 20-HETE, indicating FATP2 provides PPARα with specific proximal ligands and broadly governs hepatic lipid metabolism. FATP2-null (Fatp2-/-) mouse model, RNA-Seq transcriptomics, targeted metabolomics, RT-qPCR validation The Journal of biological chemistry Medium 32188695
2023 Arachidonic acid activates the NLRP3 inflammasome in myeloid-derived suppressor cells (MDSCs) specifically through FATP2; FATP2-mediated arachidonic acid uptake causes mitochondrial dysfunction and enhanced ROS production, which bridges lipid uptake to NLRP3 activation; activated MDSCs then stimulate CD4+ T cells to produce IL-17, promoting post-transplant tumor recurrence; blockade of FATP2 (Lipofermata) inhibits this entire axis. Lipid uptake receptor screening, mouse fatty liver ischemia-reperfusion injury model with tumor recurrence, FATP2 inhibitor (Lipofermata) treatment, NLRP3/ROS/IL-17 mechanistic assays in vitro and in vivo, clinical cohort validation JHEP reports : innovation in hepatology Medium 37916155
2023 FATP2 physically interacts with ACSL1 (long-chain acyl-CoA synthetase 1) in NSCLC cells, as demonstrated by Co-IP; FATP2 knockdown combined with ACSL1 overexpression further inhibits cell proliferation, lipid deposition, and promotes fatty acid decomposition compared to either alone, indicating FATP2 regulates lipid metabolism and cancer cell proliferation through functional interaction with ACSL1. Co-immunoprecipitation (Co-IP), siRNA knockdown, pcDNA-ACSL1 overexpression, cell proliferation assay, lipid deposition assay, ER stress markers Tissue & cell Low 37172427
2023 NRF2 directly transcriptionally activates FATP2 in the context of valproic acid (VPA)-induced hepatic steatosis: VPA binds to Cys288 and Arg415 of KEAP1, promoting autophagic KEAP1 degradation, releasing NRF2 to translocate to the nucleus where it activates FATP2 transcription, thereby enhancing fatty acid uptake and driving steatosis; this was confirmed by chromatin immunoprecipitation and dual-luciferase reporter assays, and FATP2 knockout abrogated NRF2-driven steatosis. ChIP assay, dual-luciferase reporter assay, NRF2 overexpression/knockout mice (AAV and CRISPR/Cas9), FATP2 knockout mice (homologous recombination), site-directed mutagenesis of KEAP1 binding sites, in vivo VPA treatment Theranostics High 40303331
2024 Loss of the epoxygenase Cyp2c44 (and reduced EET levels) leads to increased plasma membrane localization of FATP2 in hepatocytes, which is associated with increased total unsaturated fatty acids and diacylglycerol (DAG) accumulation, activation of PKCδ at the plasma membrane, IRS-1 serine phosphorylation, and impaired insulin signaling; treatment with the EET analog EET-A in Cyp2c44-/- HFD-fed mice decreased plasma membrane FATP2 and PKCδ levels with improved glucose tolerance, placing FATP2 membrane localization downstream of EET signaling and upstream of the DAG/PKCδ/IRS-1 axis. Cyp2c44-/- mouse model, subcellular fractionation, PKCδ inhibitor treatment, EET-A analog treatment, glucose tolerance test, lipidomics, immunoblotting Diabetes Medium 38743615
2024 FATP2 expression is upregulated during osteoclast (OC) differentiation and in bone marrow of HFD-fed mice; FATP2 siRNA or Lipofermata inhibition significantly suppresses OC differentiation with minimal effect on osteoblasts; RNA-seq shows Lipofermata reduces fatty acid β-oxidation, energy metabolism, and ROS production in OCs; in vivo Lipofermata treatment rescues bone loss in LPS-induced and ovariectomy models by inhibiting OC differentiation, establishing FATP2 as a regulator of osteoclastogenesis through fatty acid uptake and energy/ROS metabolism. siRNA knockdown, specific inhibitor (Lipofermata), RNA-seq, in vivo mouse models (LPS-induced and ovariectomy), bone mass measurement, ROS assays Journal of bone and mineral research Medium 38477781
2024 CEACAM6 promotes SLC27A2/FATP2 protein stability by interacting with both SLC27A2 and the deubiquitinase USP29; CEACAM6 facilitates USP29-mediated deubiquitination of SLC27A2, thereby upregulating fatty acid uptake and FAO in gastric cancer cells; pharmacological inhibition of SLC27A2 attenuates the tumor-initiating ability of CEACAM6-positive gastric cancer. Co-immunoprecipitation (protein-protein interaction), deubiquitination assay, SLC27A2 inhibitor (Lipofermata), in vitro and in vivo tumor models Cancer gene therapy Low 39562695
2025 In pancreatic islets, FATP2 expression is restricted to α-cells; FATP2 knockout or pharmacological inhibition (Lipofermata) in db/db mice and isolated human islets increases GLP-1-positive α-cell mass and stimulates GLP-1 secretion from α-cells; this α-cell-derived GLP-1 promotes paracrine insulin secretion from β-cells, reducing plasma glucose; the glucose-lowering effect is abrogated by GLP-1 receptor antagonism (exendin[9-39]), confirming that FATP2 inhibition acts through α-cell GLP-1 secretion rather than enteroendocrine pathways. FATP2 global KO mouse (db/db background), small molecule inhibitor (Lipofermata), GLP-1 receptor antagonist (exendin[9-39]), immunolocalization, αTC1-6 cell and human islet assays, oral vs. IP glucose challenge, mRNA co-expression analysis bioRxiv : the preprint server for biologypreprint Medium 39975070
2023 FATP2 homology model (validated by AlphaFold2 prediction and site-directed mutagenesis) was used to identify key residues for inhibitor binding; virtual screening identified two nanomolar IC50 inhibitors of FATP2-dependent fatty acid uptake and apoptosis in proximal tubule cells, providing structural insights into the FATP2 binding site. Homology modeling, AlphaFold2 structural prediction, site-directed mutagenesis, virtual docking, in vitro fatty acid uptake assay, apoptosis assay, molecular dynamics simulations International journal of biological macromolecules Low 37307967
2025 FATP2 inhibition (Lipofermata) in human monocytes reduces LPS-induced inflammatory responses and decreases biosynthesis of arachidonic acid-derived lipid mediators (PGE2, TxB2), indicating FATP2-dependent arachidonic acid uptake supports eicosanoid production; conversely, in mature monocyte-derived macrophages, Lipofermata enhances LPS-induced cytokine production and induces cell death likely through inflammasome activation, demonstrating cell type-specific roles of FATP2 in inflammatory lipid metabolism. Lipofermata inhibitor treatment, LPS stimulation, cytokine measurement, lipidomics (lipid mediator profiling), cell death assays in human monocytes and macrophages Immunology letters Low 41015393

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase. American journal of physiology. Endocrinology and metabolism 182 20530735
2020 Changes in Aged Fibroblast Lipid Metabolism Induce Age-Dependent Melanoma Cell Resistance to Targeted Therapy via the Fatty Acid Transporter FATP2. Cancer discovery 129 32499221
2011 Overexpression of CD36 and acyl-CoA synthetases FATP2, FATP4 and ACSL1 increases fatty acid uptake in human hepatoma cells. International journal of medical sciences 103 22022213
2017 Kidney Proximal Tubule Lipoapoptosis Is Regulated by Fatty Acid Transporter-2 (FATP2). Journal of the American Society of Nephrology : JASN 91 28993506
2020 Involvement of FATP2-mediated tubular lipid metabolic reprogramming in renal fibrogenesis. Cell death & disease 58 33219209
2016 Fatty Acid Transport Proteins: Targeting FATP2 as a Gatekeeper Involved in the Transport of Exogenous Fatty Acids. MedChemComm 54 27446528
2010 Slc27a2 expression in peripheral blood mononuclear cells as a molecular marker for overweight development. International journal of obesity (2005) 51 20142826
2020 FATP2-targeted therapies - A role beyond fatty liver disease. Pharmacological research 40 33027714
2020 Deletion of fatty acid transport protein 2 (FATP2) in the mouse liver changes the metabolic landscape by increasing the expression of PPARα-regulated genes. The Journal of biological chemistry 39 32188695
2013 Overexpression of human fatty acid transport protein 2/very long chain acyl-CoA synthetase 1 (FATP2/Acsvl1) reveals distinct patterns of trafficking of exogenous fatty acids. Biochemical and biophysical research communications 35 24113382
2009 Identification and characterization of small compound inhibitors of human FATP2. Biochemical pharmacology 35 19913517
2015 Reduced SLC27A2 induces cisplatin resistance in lung cancer stem cells by negatively regulating Bmi1-ABCG2 signaling. Molecular carcinogenesis 30 26513225
2018 SLC27A2 regulates miR-411 to affect chemo-resistance in ovarian cancer. Neoplasma 26 30334452
2021 Upregulated SLC27A2/FATP2 in differentiated thyroid carcinoma promotes tumor proliferation and migration. Journal of clinical laboratory analysis 24 34854499
2022 Up-regulation of SLC27A2 suppresses the proliferation and invasion of renal cancer by down-regulating CDK3-mediated EMT. Cell death discovery 20 35927229
2023 Arachidonic acid activates NLRP3 inflammasome in MDSCs via FATP2 to promote post-transplant tumour recurrence in steatotic liver grafts. JHEP reports : innovation in hepatology 17 37916155
2023 SLC27A2 mediates FAO in colorectal cancer through nongenic crosstalk regulation of the PPARs pathway. BMC cancer 16 37041476
2022 Andrographolide ameliorates hepatic steatosis by suppressing FATP2-mediated fatty acid uptake in mice with nonalcoholic fatty liver disease. Journal of natural medicines 16 36115008
2023 HBx induced upregulation of FATP2 promotes the development of hepatic lipid accumulation. Experimental cell research 15 37437769
2024 FATP2 activates PI3K/Akt/mTOR pathway by inhibiting ATF3 and promotes the occurrence and development of bladder cancer. Cellular signalling 14 38316266
2023 FATP2 regulates non-small cell lung cancer by mediating lipid metabolism through ACSL1. Tissue & cell 14 37172427
2024 SLC27A2 is a potential immune biomarker for hematological tumors and significantly regulates the cell cycle progression of diffuse large B-cell lymphoma. BMC medical genomics 13 38664735
2023 Definition of fatty acid transport protein-2 (FATP2) structure facilitates identification of small molecule inhibitors for the treatment of diabetic complications. International journal of biological macromolecules 13 37307967
2024 FATP2 regulates osteoclastogenesis by increasing lipid metabolism and ROS production. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research 11 38477781
2024 Risk assessment model based on nucleotide metabolism-related genes highlights SLC27A2 as a potential therapeutic target in breast cancer. Journal of cancer research and clinical oncology 10 38753091
2025 Long-Chain Fatty Acid Redistribution Induced by SLC27A2 Deficiency Facilitates Hypoxic Adaptation and Immunosuppression in Hepatocellular Carcinoma. Cancer research 8 40900133
2025 Mechanism of valproic acid-induced hepatic steatosis via enhancing NRF2-FATP2-mediated fatty acid uptake. Theranostics 7 40303331
2024 Epoxygenase Cyp2c44 Regulates Hepatic Lipid Metabolism and Insulin Signaling by Controlling FATP2 Localization and Activation of the DAG/PKCδ Axis. Diabetes 6 38743615
2025 SLC27A2 marks lipid peroxidation in nasal epithelial cells driven by type 2 inflammation in chronic rhinosinusitis with nasal polyps. Experimental & molecular medicine 5 40195539
2025 Semaglutide attenuates lipotoxicity-induced cardiac injury by inhibiting Slc27a2 expression. Chemico-biological interactions 3 40456371
2024 CEACAM6 facilitates gastric cancer progression through upregulating SLC27A2. Cancer gene therapy 3 39562695
2025 Fatty Acid Transport Protein-2 (FATP2) Inhibition Enhances Glucose Tolerance through α-Cell-mediated GLP-1 Secretion. bioRxiv : the preprint server for biology 2 39975070
2025 FATP2 at the crossroads of fatty acid transport, lipotoxicity, and complex disease. The Journal of clinical investigation 2 41321315
2025 Fatty acid binding protein 2 (FATP2/SLC27A2) blockade with Lipofermata elicits dual effects on inflammatory responses in human monocytes and macrophages. Immunology letters 1 41015393
2026 Adipocyte promotes tumor cell invasion and metastasis via FATP2: a novel cell-cell interaction in papillary thyroid carcinoma. Gland surgery 0 41668918
2026 Fatty acid transporter protein isoform 2 (FATP2) inhibitor lipofermata inhibits Zika virus replication and blocks fatty acid uptake in SH-SY5Y neuroblastoma cell line. Microbiology spectrum 0 41810963
2026 The FATP2 axis in cancer: Structural informatics and implications for drug discovery. Drug discovery today 0 42031099

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