{"gene":"PLIN1","run_date":"2026-06-10T06:43:35","timeline":{"discoveries":[{"year":2013,"finding":"FSP27 (CIDEC) co-localizes and physically interacts with PLIN1 in human primary adipocytes; the C-terminal domain of FSP27 (aa 120-220) mediates this interaction. Co-expression of both proteins increases average lipid droplet size and promotes formation of unilocular adipocytes, beyond the effect of either protein alone.","method":"Co-immunoprecipitation, co-localization imaging, exogenous co-expression in human primary adipocytes, glycerol release assay, triglyceride content measurement","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and co-localization with functional readout (LD size, lipolysis), single lab, two orthogonal methods","pmids":["23399566"],"is_preprint":false},{"year":2013,"finding":"In skeletal muscle, PLIN1 is absent; in adipocytes, PLIN1 is thought to regulate lipolysis by directly interacting with CGI-58, an activator of ATGL. Upon lipolytic stimulation, PLIN1 phosphorylation releases CGI-58 to fully activate ATGL and initiate triglyceride breakdown (model confirmed by analogy from adipocyte literature, tested indirectly via skeletal muscle PLIN2/3/5 interactions).","method":"Co-immunoprecipitation in isolated rat soleus muscle at rest and following tetanic stimulation","journal":"American journal of physiology. Regulatory, integrative and comparative physiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with functional stimulation, single lab; PLIN1-CGI-58 interaction in adipocytes is the established prior model referenced","pmids":["23408028"],"is_preprint":false},{"year":2014,"finding":"A novel heterozygous frameshift mutation at the carboxy-terminus (439fs) of PLIN1 produces a mutant protein at lower expression levels than wild-type; in stably transfected preadipocytes, the mutant is associated with smaller lipid droplets. Unlike previously reported frameshift mutants (398fs, 404fs), the 439fs variant retains the ability to bind and stabilize ABHD5 (CGI-58) expression but still fails to inhibit basal lipolysis as effectively as wild-type PLIN1.","method":"Stable transfection of preadipocytes, western blot for protein expression and ABHD5, lipid droplet size measurement, glycerol release lipolysis assay","journal":"Diabetes","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional mutagenesis in cell model with multiple readouts (LD size, lipolysis, ABHD5 binding), single lab","pmids":["25114292"],"is_preprint":false},{"year":1998,"finding":"The human PLIN1 gene encodes a 522 amino acid protein with 79% amino acid identity to rat perilipin; it is expressed specifically in adipose tissue among 20 human adult tissues and maps to chromosome 15q26.","method":"Differential display cDNA cloning, Northern blot, fluorescence in situ hybridization (FISH)","journal":"Genomics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct molecular characterization (cloning, expression mapping, chromosomal localization), single lab, multiple methods","pmids":["9521880"],"is_preprint":false},{"year":2019,"finding":"In C. elegans, the PLIN1 ortholog MDT-28/PLIN-1 physically binds to DLC-1 (dynein light chain) through its amino acids 1-210 and 275-415, mediating the interaction between lipid droplets and microtubules and thereby regulating lipid droplet distribution within the cell.","method":"Forward genetic screen, yeast two-hybrid, pull-down assays, fluorescence imaging of DHS-3::GFP-labeled lipid droplets","journal":"Scientific reports","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid plus pull-down plus live imaging, single lab, multiple orthogonal methods; C. elegans ortholog","pmids":["31624276"],"is_preprint":false},{"year":2017,"finding":"Promoter methylation of the PLIN1 gene is higher in adipocytes from obese women compared to never-obese women, inversely correlates with PLIN1 mRNA expression and with basal lipolysis rate. Methylation of the PLIN1 promoter directly reduces reporter gene activity in human mesenchymal stem cells differentiated into adipocytes; treatment with a DNA methyltransferase inhibitor increases PLIN1 mRNA and protein levels.","method":"CpG methylation array, correlation analysis, reporter gene (luciferase) assay with methylated vs. unmethylated promoter constructs, DNA methyltransferase inhibitor treatment, glycerol release lipolysis assay","journal":"Scientific reports","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional reporter assay plus pharmacological intervention, single lab, two orthogonal methods","pmids":["28860604"],"is_preprint":false},{"year":2020,"finding":"In bovine adipocytes, E2F1, PLAG1, C/EBPβ, and SMAD3 bind to specific sites within the core promoter region (-209/-17 bp) of the PLIN1 gene and act as transcriptional activators or repressors. Knockdown of PLIN1 affects the ability of these transcription factors to regulate lipid metabolism.","method":"Promoter deletion/luciferase reporter assays, site-directed mutagenesis, siRNA knockdown, electrophoretic mobility shift assay (EMSA)","journal":"Genomics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — EMSA and reporter assays with mutagenesis, single lab, multiple orthogonal methods","pmids":["31981700"],"is_preprint":false},{"year":2022,"finding":"PLIN1 knockout in 3T3-L1 adipocytes via CRISPR/Cas9 increases lipolysis (elevated glycerol release, decreased triglyceride content), reduces unilocular lipid droplet size, and upregulates HSL and ATGL mRNA and protein expression. PPARγ and FSP27 expression are unchanged, indicating PLIN1 regulates lipolysis by limiting lipase access to lipid droplets independently of these factors.","method":"CRISPR/Cas9 knockout, Oil Red O staining, enzymatic glycerol and triglyceride assays, Western blot, RT-PCR","journal":"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic KO with multiple mechanistic readouts, single lab","pmids":["32748596"],"is_preprint":false},{"year":2022,"finding":"PLIN1 overexpression in M1 macrophages increases lipid droplet size and reduces expression of pro-inflammatory genes (TNFA, MMP2) and cholesterol transporters (ABCA1, ABCG1). Conversely, PLIN1 silencing in M2 macrophages has opposite effects on LD size and inflammatory gene expression. PLIN1 expression on large lipid droplets is associated with an anti-inflammatory macrophage phenotype.","method":"PLIN1 overexpression and siRNA knockdown in cultured human macrophages, immunohistochemistry of carotid endarterectomy tissue, RT-PCR for inflammatory markers","journal":"Journal of atherosclerosis and thrombosis","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — gain- and loss-of-function with gene expression readouts, single lab, supported by human tissue IHC","pmids":["35662076"],"is_preprint":false},{"year":2024,"finding":"Hypertriglyceridemia in PLIN1-related familial partial lipodystrophy results from markedly impaired catabolism of VLDL and IDL (reduced indirect fractional catabolic rates), with normal VLDL-apoB100 production. Plasma LPL mass is significantly reduced in PLIN1-mutated patients despite normal LPL protein expression in adipose tissue, suggesting impaired LPL release/availability as a downstream consequence of PLIN1 dysfunction.","method":"In vivo lipoprotein kinetic study (stable isotope tracer), plasma LPL mass measurement, LPL mRNA and protein expression in adipose tissue biopsies","journal":"Arteriosclerosis, thrombosis, and vascular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo kinetic study in human patients with mechanistic readouts, single study, multiple methods","pmids":["38899472"],"is_preprint":false},{"year":2025,"finding":"The C-terminal end of mouse PLIN1 (mPLIN1C) behaves as an intrinsically disordered region (IDR) of the coil-like or pre-molten globule type. Interaction with SDS micelles induces a conformational transition toward a pre-molten globule state. Molecular recognition feature (MoRF) analysis identifies the EPESE sequence (residues 413-417) as a potential binding site for partner molecules including CGI-58.","method":"Circular dichroism spectroscopy, SDS micelle interaction assays, bioinformatic disorder prediction, MoRF analysis","journal":"Biochemistry and biophysics reports","confidence":"Low","confidence_rationale":"Tier 3 / Weak — biophysical characterization of recombinant C-terminal fragment, single lab, no functional mutagenesis validation","pmids":["40109298"],"is_preprint":false},{"year":2019,"finding":"In chicken, RXRα activates transcription of the PLIN1 gene in a PPARγ-independent manner by binding to a specific site in the PLIN1 promoter region (-774/-785 bp). RXRα overexpression promotes preadipocyte differentiation with concomitant increase in PLIN1 transcripts.","method":"Reporter gene assays, promoter deletion analysis, EMSA, RXRα overexpression in immortalized chicken preadipocyte line (ICP1)","journal":"Frontiers in cell and developmental biology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — EMSA and reporter assay in chicken cells, single lab, functional link to adipogenesis but not mammalian PLIN1 directly","pmids":["32478078"],"is_preprint":false},{"year":2025,"finding":"Seipin (BSCL2) is required for recruiting PLIN1 to the lipid droplet surface in human adipocytes but is dispensable for lipid droplet biogenesis itself. Loss of seipin-dependent PLIN1 recruitment leads to enhanced lipolysis, ceramide accumulation, and de-differentiation of adipocytes into a progenitor-like state. This identifies PLIN1 recruitment as a seipin-dependent quality-control checkpoint enforcing adipocyte identity.","method":"BSCL2 knockout in human adipocyte progenitor cells, in vitro and in vivo differentiation assays, lipolysis measurement, ceramide quantification, live-cell imaging, xenograft experiments","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic KO with multiple orthogonal functional readouts (lipolysis, ceramide, de-differentiation, in vivo), preprint single lab","pmids":[],"is_preprint":true},{"year":2024,"finding":"During differentiation of 3T3-L1 preadipocytes into adipocytes, PLIN1 becomes a high-affinity lipid droplet protein that is extensively recruited to the LD surface and displaces lower-affinity ER proteins via lateral steric exclusion, remodeling the LD proteome.","method":"Ex vivo ER-to-LD partitioning assay, fluorescence microscopy, quantitative protein localization during adipocyte differentiation","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single preprint lab, descriptive localization during differentiation without direct mutagenesis of PLIN1","pmids":[],"is_preprint":true},{"year":2022,"finding":"PLIN1 knockout and overexpression in porcine skeletal muscle satellite cells both enhance anti-apoptotic ability and accelerate metabolic activity, but at the cost of mitochondrial structural damage, reduced mitochondrial number, and decreased mitochondrial function, indicating PLIN1 stable expression is required for normal mitochondrial homeostasis in these cells.","method":"CRISPR/Cas9 knockout, adenoviral overexpression, flow cytometry (apoptosis, cell cycle), western blot for mitochondrial proteins, electron microscopy","journal":"Genes & genomics","confidence":"Low","confidence_rationale":"Tier 3 / Weak — gain- and loss-of-function in non-adipocyte cell type (skeletal muscle satellite cells), single lab, limited mechanistic pathway placement","pmids":["35438463"],"is_preprint":false},{"year":2025,"finding":"Runx1 transcription factor promotes the transformation of adipocytes into cancer-associated adipocytes (CAAs) by downregulating Plin1 expression. Overexpression of Plin1 in adipocytes inhibits the Runx1-driven transition to CAAs and reduces enhancement of breast cancer cell migration and invasion.","method":"Co-culture system of mature adipocytes and breast cancer cells, RNA sequencing, Runx1 overexpression/knockdown in 3T3-L1 preadipocytes, Plin1 overexpression rescue experiments, migration/invasion assays","journal":"Experimental cell research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, rescue experiment with Plin1 overexpression but limited mechanistic detail on how Runx1 regulates Plin1","pmids":["40280321"],"is_preprint":false},{"year":2025,"finding":"In glioma cells, the PI3K/AKT signaling axis negatively regulates PLIN1 levels; pharmacological inhibition of PI3K/AKT activity increases PLIN1 expression, which in turn suppresses cell growth and invasion and increases lipid accumulation with upregulation of lipid biosynthesis genes and downregulation of lipolysis genes.","method":"PI3K/AKT inhibitor treatment, PLIN1 overexpression, RNA-seq, cell proliferation and invasion assays","journal":"Cell death & disease","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, pathway placement by pharmacological inhibition without genetic epistasis confirmation","pmids":["39870645"],"is_preprint":false}],"current_model":"PLIN1 (perilipin-1) is a lipid droplet coat protein predominantly expressed in adipocytes that inhibits basal lipolysis by limiting lipase access to stored triglycerides, and facilitates stimulated lipolysis through PKA-mediated phosphorylation that releases CGI-58 (ABHD5) to fully activate ATGL; it physically interacts with FSP27/CIDEC to regulate lipid droplet size, requires seipin (BSCL2) for recruitment to the lipid droplet surface, and its C-terminal intrinsically disordered region mediates interactions with co-regulators including CGI-58, while loss-of-function frameshift mutations that extend the C-terminus cause familial partial lipodystrophy by impairing basal lipolysis suppression."},"narrative":{"mechanistic_narrative":"PLIN1 (perilipin-1) is an adipose-specific lipid droplet coat protein that controls triglyceride storage and mobilization by gating lipase access to the droplet core [PMID:9521880, PMID:32748596]. CRISPR knockout in adipocytes elevates lipolysis and upregulates HSL and ATGL while leaving PPARγ and FSP27 unchanged, establishing that PLIN1 suppresses basal lipolysis by limiting lipase access rather than through these factors [PMID:32748596]. PLIN1 physically interacts with CGI-58 (ABHD5), an ATGL activator, and stabilizes its expression; this interaction is mediated by the protein's C-terminal region, which behaves as an intrinsically disordered domain containing a candidate molecular-recognition motif (EPESE, residues 413-417) for CGI-58 binding [PMID:23408028, PMID:25114292, PMID:40109298]. PLIN1 also co-localizes and physically interacts with FSP27/CIDEC via the CIDEC C-terminus, and their co-expression enlarges lipid droplets and promotes unilocular adipocyte morphology [PMID:23399566]. Recruitment of PLIN1 to the lipid droplet surface requires seipin (BSCL2) and reflects PLIN1's high affinity for the droplet surface, where it laterally displaces lower-affinity proteins and remodels the droplet proteome; loss of this recruitment enhances lipolysis and drives adipocyte de-differentiation. C-terminal frameshift mutations that extend the protein impair suppression of basal lipolysis and cause familial partial lipodystrophy, with affected patients showing impaired VLDL/IDL catabolism and reduced plasma LPL availability [PMID:25114292, PMID:38899472]. PLIN1 transcription is controlled by promoter methylation and by transcription factors including E2F1, PLAG1, C/EBPβ and SMAD3 [PMID:28860604, PMID:31981700].","teleology":[{"year":1998,"claim":"Establishing PLIN1 as a distinct human gene with adipose-restricted expression set the foundation for studying it as an adipocyte-specific lipid droplet regulator.","evidence":"cDNA cloning, Northern blot across 20 tissues, and FISH mapping to 15q26","pmids":["9521880"],"confidence":"Medium","gaps":["No functional mechanism defined at this stage","Protein localization to lipid droplets not directly demonstrated here"]},{"year":2013,"claim":"Identifying a direct PLIN1-FSP27/CIDEC interaction explained how PLIN1 contributes to lipid droplet enlargement and unilocular adipocyte morphology, mapping the interaction to the CIDEC C-terminus.","evidence":"Reciprocal Co-IP, co-localization, and co-expression with LD-size and lipolysis readouts in human primary adipocytes","pmids":["23399566"],"confidence":"Medium","gaps":["PLIN1 region mediating the interaction not mapped","Stoichiometry and structural basis unknown"]},{"year":2013,"claim":"Co-IP testing of the perilipin-CGI-58 model placed PLIN1's regulation of lipolysis in the framework of phosphorylation-triggered CGI-58 release to activate ATGL.","evidence":"Reciprocal Co-IP in rat soleus muscle at rest and after tetanic stimulation, referencing the adipocyte PLIN1-CGI-58 model","pmids":["23408028"],"confidence":"Medium","gaps":["PLIN1 absent in skeletal muscle, so the adipocyte interaction is inferred by analogy","Direct phosphorylation-dependent release not measured for PLIN1 itself here"]},{"year":2014,"claim":"Functional dissection of a C-terminal frameshift mutant showed that ABHD5/CGI-58 binding can be retained yet basal lipolysis suppression still lost, separating CGI-58 stabilization from lipolytic control and linking C-terminal integrity to lipodystrophy.","evidence":"Stable transfection of preadipocytes with 439fs mutant, Western blot for ABHD5, LD-size and glycerol-release assays","pmids":["25114292"],"confidence":"Medium","gaps":["Molecular mechanism by which the extended C-terminus impairs lipolysis control unresolved","Single cell-model system"]},{"year":2017,"claim":"Demonstrating that promoter methylation represses PLIN1 and correlates with basal lipolysis added an epigenetic layer of control over PLIN1 abundance in obesity.","evidence":"CpG methylation array, methylated/unmethylated luciferase reporter assays, DNMT inhibitor treatment, glycerol release in human MSC-derived adipocytes","pmids":["28860604"],"confidence":"Medium","gaps":["Specific methyltransferases and signals driving methylation not identified","Correlational link to lipolysis rate"]},{"year":2020,"claim":"Mapping E2F1, PLAG1, C/EBPβ and SMAD3 to the PLIN1 core promoter defined the transcriptional circuitry controlling PLIN1 expression and downstream lipid metabolism.","evidence":"Promoter deletion/luciferase assays, site-directed mutagenesis, EMSA, siRNA knockdown in bovine adipocytes","pmids":["31981700"],"confidence":"Medium","gaps":["Activator vs repressor roles of individual factors not fully resolved","Bovine system; human conservation not tested"]},{"year":2022,"claim":"CRISPR knockout in adipocytes established causally that PLIN1 suppresses basal lipolysis by limiting lipase access, independently of PPARγ and FSP27.","evidence":"CRISPR/Cas9 KO in 3T3-L1, Oil Red O, glycerol/triglyceride assays, Western blot and RT-PCR for HSL/ATGL/PPARγ/FSP27","pmids":["32748596"],"confidence":"Medium","gaps":["Mechanism of lipase exclusion at the molecular level not resolved","Stimulated lipolysis arm not dissected here"]},{"year":2022,"claim":"Gain/loss-of-function in macrophages extended PLIN1 function beyond adipocytes, linking PLIN1-coated large lipid droplets to an anti-inflammatory phenotype.","evidence":"Overexpression and siRNA in human macrophages, RT-PCR for inflammatory and cholesterol-transport genes, carotid plaque IHC","pmids":["35662076"],"confidence":"Medium","gaps":["Mechanism connecting LD size to inflammatory gene expression unknown","Causality in vivo not established"]},{"year":2024,"claim":"In vivo kinetic study in lipodystrophy patients traced PLIN1 dysfunction to systemic consequences, showing impaired VLDL/IDL catabolism and reduced plasma LPL availability.","evidence":"Stable-isotope lipoprotein kinetics, plasma LPL mass, adipose LPL mRNA/protein in PLIN1-mutated patients","pmids":["38899472"],"confidence":"Medium","gaps":["Mechanistic link between adipocyte PLIN1 loss and reduced LPL release not defined","Small patient cohort"]},{"year":2025,"claim":"Identifying seipin as required for PLIN1 recruitment to the droplet surface placed PLIN1 loading as a quality-control checkpoint enforcing adipocyte identity.","evidence":"BSCL2 KO in human adipocyte progenitors, differentiation, lipolysis and ceramide assays, live imaging, xenografts (preprint)","pmids":[],"confidence":"Medium","gaps":["Direct seipin-PLIN1 interaction vs indirect recruitment not distinguished","Preprint, single lab"]},{"year":2025,"claim":"Biophysical characterization defined the PLIN1 C-terminus as an intrinsically disordered region with a candidate CGI-58 binding motif, providing a structural basis for its co-regulator interactions.","evidence":"Circular dichroism, SDS-micelle conformational assays, disorder prediction and MoRF analysis on recombinant mouse C-terminal fragment","pmids":["40109298"],"confidence":"Low","gaps":["No functional mutagenesis validating the EPESE motif","Isolated fragment, not full-length protein in cells"]},{"year":null,"claim":"How PLIN1 phosphorylation, CGI-58 release, and the disordered C-terminus mechanistically coordinate the switch from basal lipolysis suppression to stimulated lipolysis remains to be reconstituted.","evidence":"No direct timeline finding resolves the integrated phosphorylation-to-lipolysis mechanism","pmids":[],"confidence":"Low","gaps":["No structural model of PLIN1 on the droplet surface bound to partners","Lipase-exclusion mechanism uncharacterized at molecular resolution"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[1,2,7]},{"term_id":"GO:0008289","term_label":"lipid binding","supporting_discovery_ids":[13]}],"localization":[{"term_id":"GO:0005811","term_label":"lipid droplet","supporting_discovery_ids":[0,12,13]}],"pathway":[{"term_id":"R-HSA-1430728","term_label":"Metabolism","supporting_discovery_ids":[7,9]}],"complexes":[],"partners":["CIDEC","ABHD5","BSCL2","DLC-1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O60240","full_name":"Perilipin-1","aliases":["Lipid droplet-associated protein"],"length_aa":522,"mass_kda":56.0,"function":"Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels","subcellular_location":"Endoplasmic reticulum; Lipid droplet","url":"https://www.uniprot.org/uniprotkb/O60240/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/PLIN1","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/PLIN1","total_profiled":1310},"omim":[{"mim_id":"619894","title":"ABHYDROLASE DOMAIN-CONTAINING PROTEIN 15; ABHD15","url":"https://www.omim.org/entry/619894"},{"mim_id":"613877","title":"LIPODYSTROPHY, FAMILIAL PARTIAL, TYPE 4; FPLD4","url":"https://www.omim.org/entry/613877"},{"mim_id":"613248","title":"PERILIPIN 5; PLIN5","url":"https://www.omim.org/entry/613248"},{"mim_id":"613247","title":"PERILIPIN 4; PLIN4","url":"https://www.omim.org/entry/613247"},{"mim_id":"609888","title":"LEPROSY, SUSCEPTIBILITY TO, 1; LPRS1","url":"https://www.omim.org/entry/609888"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Uncertain","locations":[{"location":"Peroxisomes","reliability":"Uncertain"}],"tissue_specificity":"Group enriched","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"adipose tissue","ntpm":898.1},{"tissue":"breast","ntpm":459.5}],"url":"https://www.proteinatlas.org/search/PLIN1"},"hgnc":{"alias_symbol":[],"prev_symbol":["PLIN"]},"alphafold":{"accession":"O60240","domains":[{"cath_id":"-","chopping":"21-107","consensus_level":"high","plddt":72.2724,"start":21,"end":107},{"cath_id":"-","chopping":"183-194_219-248","consensus_level":"medium","plddt":70.7583,"start":183,"end":248}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O60240","model_url":"https://alphafold.ebi.ac.uk/files/AF-O60240-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O60240-F1-predicted_aligned_error_v6.png","plddt_mean":54.69},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=PLIN1","jax_strain_url":"https://www.jax.org/strain/search?query=PLIN1"},"sequence":{"accession":"O60240","fasta_url":"https://rest.uniprot.org/uniprotkb/O60240.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O60240/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O60240"}},"corpus_meta":[{"pmid":"23399566","id":"PMC_23399566","title":"FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes.","date":"2013","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/23399566","citation_count":113,"is_preprint":false},{"pmid":"15355432","id":"PMC_15355432","title":"Genetic variation at the perilipin (PLIN) locus is associated with obesity-related phenotypes in White women.","date":"2004","source":"Clinical genetics","url":"https://pubmed.ncbi.nlm.nih.gov/15355432","citation_count":83,"is_preprint":false},{"pmid":"23408028","id":"PMC_23408028","title":"Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and following stimulated contraction.","date":"2013","source":"American journal of physiology. Regulatory, integrative and comparative physiology","url":"https://pubmed.ncbi.nlm.nih.gov/23408028","citation_count":76,"is_preprint":false},{"pmid":"25114292","id":"PMC_25114292","title":"Clinical and molecular characterization of a novel PLIN1 frameshift mutation identified in patients with familial partial lipodystrophy.","date":"2014","source":"Diabetes","url":"https://pubmed.ncbi.nlm.nih.gov/25114292","citation_count":64,"is_preprint":false},{"pmid":"22667335","id":"PMC_22667335","title":"Perilipin family (PLIN) proteins in human skeletal muscle: the effect of sex, obesity, and endurance training.","date":"2012","source":"Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme","url":"https://pubmed.ncbi.nlm.nih.gov/22667335","citation_count":61,"is_preprint":false},{"pmid":"29617344","id":"PMC_29617344","title":"A Key Gene, PLIN1, Can Affect Porcine Intramuscular Fat Content Based on Transcriptome Analysis.","date":"2018","source":"Genes","url":"https://pubmed.ncbi.nlm.nih.gov/29617344","citation_count":57,"is_preprint":false},{"pmid":"15770500","id":"PMC_15770500","title":"Intragenic linkage disequilibrium structure of the human perilipin gene (PLIN) and haplotype association with increased obesity risk in a multiethnic Asian population.","date":"2005","source":"Journal of molecular medicine (Berlin, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/15770500","citation_count":56,"is_preprint":false},{"pmid":"33105676","id":"PMC_33105676","title":"Overexpression of PLIN1 Promotes Lipid Metabolism in Bovine Adipocytes.","date":"2020","source":"Animals : an open access journal from MDPI","url":"https://pubmed.ncbi.nlm.nih.gov/33105676","citation_count":38,"is_preprint":false},{"pmid":"31981700","id":"PMC_31981700","title":"Function and characterization of the promoter region of perilipin 1 (PLIN1): Roles of E2F1, PLAG1, C/EBPβ, and SMAD3 in bovine adipocytes.","date":"2020","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/31981700","citation_count":37,"is_preprint":false},{"pmid":"32012433","id":"PMC_32012433","title":"Plin-amiR, a pre-microRNA-based technology for controlling herbivorous insect pests.","date":"2020","source":"Plant biotechnology journal","url":"https://pubmed.ncbi.nlm.nih.gov/32012433","citation_count":36,"is_preprint":false},{"pmid":"18812483","id":"PMC_18812483","title":"Effects of perilipin (PLIN) gene variation on metabolic syndrome risk and weight loss in obese children and adolescents.","date":"2008","source":"The Journal of clinical endocrinology and metabolism","url":"https://pubmed.ncbi.nlm.nih.gov/18812483","citation_count":33,"is_preprint":false},{"pmid":"31504636","id":"PMC_31504636","title":"Diagnostic Challenge in PLIN1-Associated Familial Partial Lipodystrophy.","date":"2019","source":"The Journal of clinical endocrinology and metabolism","url":"https://pubmed.ncbi.nlm.nih.gov/31504636","citation_count":31,"is_preprint":false},{"pmid":"9521880","id":"PMC_9521880","title":"Isolation and chromosomal mapping of the human homolog of perilipin (PLIN), a rat adipose tissue-specific gene, by differential display method.","date":"1998","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/9521880","citation_count":31,"is_preprint":false},{"pmid":"32110804","id":"PMC_32110804","title":"Long non-coding RNA ARAP1-AS1 accelerates cell proliferation and migration in breast cancer through miR-2110/HDAC2/PLIN1 axis.","date":"2020","source":"Bioscience reports","url":"https://pubmed.ncbi.nlm.nih.gov/32110804","citation_count":29,"is_preprint":false},{"pmid":"22012700","id":"PMC_22012700","title":"Subcellular localization of skeletal muscle lipid droplets and PLIN family proteins OXPAT and ADRP at rest and following contraction in rat soleus muscle.","date":"2011","source":"American journal of physiology. 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Co-expression of both proteins increases average lipid droplet size and promotes formation of unilocular adipocytes, beyond the effect of either protein alone.\",\n      \"method\": \"Co-immunoprecipitation, co-localization imaging, exogenous co-expression in human primary adipocytes, glycerol release assay, triglyceride content measurement\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and co-localization with functional readout (LD size, lipolysis), single lab, two orthogonal methods\",\n      \"pmids\": [\"23399566\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"In skeletal muscle, PLIN1 is absent; in adipocytes, PLIN1 is thought to regulate lipolysis by directly interacting with CGI-58, an activator of ATGL. Upon lipolytic stimulation, PLIN1 phosphorylation releases CGI-58 to fully activate ATGL and initiate triglyceride breakdown (model confirmed by analogy from adipocyte literature, tested indirectly via skeletal muscle PLIN2/3/5 interactions).\",\n      \"method\": \"Co-immunoprecipitation in isolated rat soleus muscle at rest and following tetanic stimulation\",\n      \"journal\": \"American journal of physiology. Regulatory, integrative and comparative physiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with functional stimulation, single lab; PLIN1-CGI-58 interaction in adipocytes is the established prior model referenced\",\n      \"pmids\": [\"23408028\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"A novel heterozygous frameshift mutation at the carboxy-terminus (439fs) of PLIN1 produces a mutant protein at lower expression levels than wild-type; in stably transfected preadipocytes, the mutant is associated with smaller lipid droplets. Unlike previously reported frameshift mutants (398fs, 404fs), the 439fs variant retains the ability to bind and stabilize ABHD5 (CGI-58) expression but still fails to inhibit basal lipolysis as effectively as wild-type PLIN1.\",\n      \"method\": \"Stable transfection of preadipocytes, western blot for protein expression and ABHD5, lipid droplet size measurement, glycerol release lipolysis assay\",\n      \"journal\": \"Diabetes\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional mutagenesis in cell model with multiple readouts (LD size, lipolysis, ABHD5 binding), single lab\",\n      \"pmids\": [\"25114292\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1998,\n      \"finding\": \"The human PLIN1 gene encodes a 522 amino acid protein with 79% amino acid identity to rat perilipin; it is expressed specifically in adipose tissue among 20 human adult tissues and maps to chromosome 15q26.\",\n      \"method\": \"Differential display cDNA cloning, Northern blot, fluorescence in situ hybridization (FISH)\",\n      \"journal\": \"Genomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct molecular characterization (cloning, expression mapping, chromosomal localization), single lab, multiple methods\",\n      \"pmids\": [\"9521880\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"In C. elegans, the PLIN1 ortholog MDT-28/PLIN-1 physically binds to DLC-1 (dynein light chain) through its amino acids 1-210 and 275-415, mediating the interaction between lipid droplets and microtubules and thereby regulating lipid droplet distribution within the cell.\",\n      \"method\": \"Forward genetic screen, yeast two-hybrid, pull-down assays, fluorescence imaging of DHS-3::GFP-labeled lipid droplets\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid plus pull-down plus live imaging, single lab, multiple orthogonal methods; C. elegans ortholog\",\n      \"pmids\": [\"31624276\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Promoter methylation of the PLIN1 gene is higher in adipocytes from obese women compared to never-obese women, inversely correlates with PLIN1 mRNA expression and with basal lipolysis rate. Methylation of the PLIN1 promoter directly reduces reporter gene activity in human mesenchymal stem cells differentiated into adipocytes; treatment with a DNA methyltransferase inhibitor increases PLIN1 mRNA and protein levels.\",\n      \"method\": \"CpG methylation array, correlation analysis, reporter gene (luciferase) assay with methylated vs. unmethylated promoter constructs, DNA methyltransferase inhibitor treatment, glycerol release lipolysis assay\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional reporter assay plus pharmacological intervention, single lab, two orthogonal methods\",\n      \"pmids\": [\"28860604\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"In bovine adipocytes, E2F1, PLAG1, C/EBPβ, and SMAD3 bind to specific sites within the core promoter region (-209/-17 bp) of the PLIN1 gene and act as transcriptional activators or repressors. Knockdown of PLIN1 affects the ability of these transcription factors to regulate lipid metabolism.\",\n      \"method\": \"Promoter deletion/luciferase reporter assays, site-directed mutagenesis, siRNA knockdown, electrophoretic mobility shift assay (EMSA)\",\n      \"journal\": \"Genomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — EMSA and reporter assays with mutagenesis, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"31981700\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PLIN1 knockout in 3T3-L1 adipocytes via CRISPR/Cas9 increases lipolysis (elevated glycerol release, decreased triglyceride content), reduces unilocular lipid droplet size, and upregulates HSL and ATGL mRNA and protein expression. PPARγ and FSP27 expression are unchanged, indicating PLIN1 regulates lipolysis by limiting lipase access to lipid droplets independently of these factors.\",\n      \"method\": \"CRISPR/Cas9 knockout, Oil Red O staining, enzymatic glycerol and triglyceride assays, Western blot, RT-PCR\",\n      \"journal\": \"Sheng wu gong cheng xue bao = Chinese journal of biotechnology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic KO with multiple mechanistic readouts, single lab\",\n      \"pmids\": [\"32748596\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PLIN1 overexpression in M1 macrophages increases lipid droplet size and reduces expression of pro-inflammatory genes (TNFA, MMP2) and cholesterol transporters (ABCA1, ABCG1). Conversely, PLIN1 silencing in M2 macrophages has opposite effects on LD size and inflammatory gene expression. PLIN1 expression on large lipid droplets is associated with an anti-inflammatory macrophage phenotype.\",\n      \"method\": \"PLIN1 overexpression and siRNA knockdown in cultured human macrophages, immunohistochemistry of carotid endarterectomy tissue, RT-PCR for inflammatory markers\",\n      \"journal\": \"Journal of atherosclerosis and thrombosis\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — gain- and loss-of-function with gene expression readouts, single lab, supported by human tissue IHC\",\n      \"pmids\": [\"35662076\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Hypertriglyceridemia in PLIN1-related familial partial lipodystrophy results from markedly impaired catabolism of VLDL and IDL (reduced indirect fractional catabolic rates), with normal VLDL-apoB100 production. Plasma LPL mass is significantly reduced in PLIN1-mutated patients despite normal LPL protein expression in adipose tissue, suggesting impaired LPL release/availability as a downstream consequence of PLIN1 dysfunction.\",\n      \"method\": \"In vivo lipoprotein kinetic study (stable isotope tracer), plasma LPL mass measurement, LPL mRNA and protein expression in adipose tissue biopsies\",\n      \"journal\": \"Arteriosclerosis, thrombosis, and vascular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo kinetic study in human patients with mechanistic readouts, single study, multiple methods\",\n      \"pmids\": [\"38899472\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"The C-terminal end of mouse PLIN1 (mPLIN1C) behaves as an intrinsically disordered region (IDR) of the coil-like or pre-molten globule type. Interaction with SDS micelles induces a conformational transition toward a pre-molten globule state. Molecular recognition feature (MoRF) analysis identifies the EPESE sequence (residues 413-417) as a potential binding site for partner molecules including CGI-58.\",\n      \"method\": \"Circular dichroism spectroscopy, SDS micelle interaction assays, bioinformatic disorder prediction, MoRF analysis\",\n      \"journal\": \"Biochemistry and biophysics reports\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — biophysical characterization of recombinant C-terminal fragment, single lab, no functional mutagenesis validation\",\n      \"pmids\": [\"40109298\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"In chicken, RXRα activates transcription of the PLIN1 gene in a PPARγ-independent manner by binding to a specific site in the PLIN1 promoter region (-774/-785 bp). RXRα overexpression promotes preadipocyte differentiation with concomitant increase in PLIN1 transcripts.\",\n      \"method\": \"Reporter gene assays, promoter deletion analysis, EMSA, RXRα overexpression in immortalized chicken preadipocyte line (ICP1)\",\n      \"journal\": \"Frontiers in cell and developmental biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — EMSA and reporter assay in chicken cells, single lab, functional link to adipogenesis but not mammalian PLIN1 directly\",\n      \"pmids\": [\"32478078\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Seipin (BSCL2) is required for recruiting PLIN1 to the lipid droplet surface in human adipocytes but is dispensable for lipid droplet biogenesis itself. Loss of seipin-dependent PLIN1 recruitment leads to enhanced lipolysis, ceramide accumulation, and de-differentiation of adipocytes into a progenitor-like state. This identifies PLIN1 recruitment as a seipin-dependent quality-control checkpoint enforcing adipocyte identity.\",\n      \"method\": \"BSCL2 knockout in human adipocyte progenitor cells, in vitro and in vivo differentiation assays, lipolysis measurement, ceramide quantification, live-cell imaging, xenograft experiments\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic KO with multiple orthogonal functional readouts (lipolysis, ceramide, de-differentiation, in vivo), preprint single lab\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"During differentiation of 3T3-L1 preadipocytes into adipocytes, PLIN1 becomes a high-affinity lipid droplet protein that is extensively recruited to the LD surface and displaces lower-affinity ER proteins via lateral steric exclusion, remodeling the LD proteome.\",\n      \"method\": \"Ex vivo ER-to-LD partitioning assay, fluorescence microscopy, quantitative protein localization during adipocyte differentiation\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single preprint lab, descriptive localization during differentiation without direct mutagenesis of PLIN1\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PLIN1 knockout and overexpression in porcine skeletal muscle satellite cells both enhance anti-apoptotic ability and accelerate metabolic activity, but at the cost of mitochondrial structural damage, reduced mitochondrial number, and decreased mitochondrial function, indicating PLIN1 stable expression is required for normal mitochondrial homeostasis in these cells.\",\n      \"method\": \"CRISPR/Cas9 knockout, adenoviral overexpression, flow cytometry (apoptosis, cell cycle), western blot for mitochondrial proteins, electron microscopy\",\n      \"journal\": \"Genes & genomics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — gain- and loss-of-function in non-adipocyte cell type (skeletal muscle satellite cells), single lab, limited mechanistic pathway placement\",\n      \"pmids\": [\"35438463\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Runx1 transcription factor promotes the transformation of adipocytes into cancer-associated adipocytes (CAAs) by downregulating Plin1 expression. Overexpression of Plin1 in adipocytes inhibits the Runx1-driven transition to CAAs and reduces enhancement of breast cancer cell migration and invasion.\",\n      \"method\": \"Co-culture system of mature adipocytes and breast cancer cells, RNA sequencing, Runx1 overexpression/knockdown in 3T3-L1 preadipocytes, Plin1 overexpression rescue experiments, migration/invasion assays\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, rescue experiment with Plin1 overexpression but limited mechanistic detail on how Runx1 regulates Plin1\",\n      \"pmids\": [\"40280321\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"In glioma cells, the PI3K/AKT signaling axis negatively regulates PLIN1 levels; pharmacological inhibition of PI3K/AKT activity increases PLIN1 expression, which in turn suppresses cell growth and invasion and increases lipid accumulation with upregulation of lipid biosynthesis genes and downregulation of lipolysis genes.\",\n      \"method\": \"PI3K/AKT inhibitor treatment, PLIN1 overexpression, RNA-seq, cell proliferation and invasion assays\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, pathway placement by pharmacological inhibition without genetic epistasis confirmation\",\n      \"pmids\": [\"39870645\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"PLIN1 (perilipin-1) is a lipid droplet coat protein predominantly expressed in adipocytes that inhibits basal lipolysis by limiting lipase access to stored triglycerides, and facilitates stimulated lipolysis through PKA-mediated phosphorylation that releases CGI-58 (ABHD5) to fully activate ATGL; it physically interacts with FSP27/CIDEC to regulate lipid droplet size, requires seipin (BSCL2) for recruitment to the lipid droplet surface, and its C-terminal intrinsically disordered region mediates interactions with co-regulators including CGI-58, while loss-of-function frameshift mutations that extend the C-terminus cause familial partial lipodystrophy by impairing basal lipolysis suppression.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PLIN1 (perilipin-1) is an adipose-specific lipid droplet coat protein that controls triglyceride storage and mobilization by gating lipase access to the droplet core [#3, #7]. CRISPR knockout in adipocytes elevates lipolysis and upregulates HSL and ATGL while leaving PPARγ and FSP27 unchanged, establishing that PLIN1 suppresses basal lipolysis by limiting lipase access rather than through these factors [#7]. PLIN1 physically interacts with CGI-58 (ABHD5), an ATGL activator, and stabilizes its expression; this interaction is mediated by the protein's C-terminal region, which behaves as an intrinsically disordered domain containing a candidate molecular-recognition motif (EPESE, residues 413-417) for CGI-58 binding [#1, #2, #10]. PLIN1 also co-localizes and physically interacts with FSP27/CIDEC via the CIDEC C-terminus, and their co-expression enlarges lipid droplets and promotes unilocular adipocyte morphology [#0]. Recruitment of PLIN1 to the lipid droplet surface requires seipin (BSCL2) and reflects PLIN1's high affinity for the droplet surface, where it laterally displaces lower-affinity proteins and remodels the droplet proteome; loss of this recruitment enhances lipolysis and drives adipocyte de-differentiation [#12, #13]. C-terminal frameshift mutations that extend the protein impair suppression of basal lipolysis and cause familial partial lipodystrophy, with affected patients showing impaired VLDL/IDL catabolism and reduced plasma LPL availability [#2, #9]. PLIN1 transcription is controlled by promoter methylation and by transcription factors including E2F1, PLAG1, C/EBPβ and SMAD3 [#5, #6].\",\n  \"teleology\": [\n    {\n      \"year\": 1998,\n      \"claim\": \"Establishing PLIN1 as a distinct human gene with adipose-restricted expression set the foundation for studying it as an adipocyte-specific lipid droplet regulator.\",\n      \"evidence\": \"cDNA cloning, Northern blot across 20 tissues, and FISH mapping to 15q26\",\n      \"pmids\": [\"9521880\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No functional mechanism defined at this stage\", \"Protein localization to lipid droplets not directly demonstrated here\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Identifying a direct PLIN1-FSP27/CIDEC interaction explained how PLIN1 contributes to lipid droplet enlargement and unilocular adipocyte morphology, mapping the interaction to the CIDEC C-terminus.\",\n      \"evidence\": \"Reciprocal Co-IP, co-localization, and co-expression with LD-size and lipolysis readouts in human primary adipocytes\",\n      \"pmids\": [\"23399566\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"PLIN1 region mediating the interaction not mapped\", \"Stoichiometry and structural basis unknown\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Co-IP testing of the perilipin-CGI-58 model placed PLIN1's regulation of lipolysis in the framework of phosphorylation-triggered CGI-58 release to activate ATGL.\",\n      \"evidence\": \"Reciprocal Co-IP in rat soleus muscle at rest and after tetanic stimulation, referencing the adipocyte PLIN1-CGI-58 model\",\n      \"pmids\": [\"23408028\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"PLIN1 absent in skeletal muscle, so the adipocyte interaction is inferred by analogy\", \"Direct phosphorylation-dependent release not measured for PLIN1 itself here\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Functional dissection of a C-terminal frameshift mutant showed that ABHD5/CGI-58 binding can be retained yet basal lipolysis suppression still lost, separating CGI-58 stabilization from lipolytic control and linking C-terminal integrity to lipodystrophy.\",\n      \"evidence\": \"Stable transfection of preadipocytes with 439fs mutant, Western blot for ABHD5, LD-size and glycerol-release assays\",\n      \"pmids\": [\"25114292\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular mechanism by which the extended C-terminus impairs lipolysis control unresolved\", \"Single cell-model system\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrating that promoter methylation represses PLIN1 and correlates with basal lipolysis added an epigenetic layer of control over PLIN1 abundance in obesity.\",\n      \"evidence\": \"CpG methylation array, methylated/unmethylated luciferase reporter assays, DNMT inhibitor treatment, glycerol release in human MSC-derived adipocytes\",\n      \"pmids\": [\"28860604\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Specific methyltransferases and signals driving methylation not identified\", \"Correlational link to lipolysis rate\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Mapping E2F1, PLAG1, C/EBPβ and SMAD3 to the PLIN1 core promoter defined the transcriptional circuitry controlling PLIN1 expression and downstream lipid metabolism.\",\n      \"evidence\": \"Promoter deletion/luciferase assays, site-directed mutagenesis, EMSA, siRNA knockdown in bovine adipocytes\",\n      \"pmids\": [\"31981700\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Activator vs repressor roles of individual factors not fully resolved\", \"Bovine system; human conservation not tested\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"CRISPR knockout in adipocytes established causally that PLIN1 suppresses basal lipolysis by limiting lipase access, independently of PPARγ and FSP27.\",\n      \"evidence\": \"CRISPR/Cas9 KO in 3T3-L1, Oil Red O, glycerol/triglyceride assays, Western blot and RT-PCR for HSL/ATGL/PPARγ/FSP27\",\n      \"pmids\": [\"32748596\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism of lipase exclusion at the molecular level not resolved\", \"Stimulated lipolysis arm not dissected here\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Gain/loss-of-function in macrophages extended PLIN1 function beyond adipocytes, linking PLIN1-coated large lipid droplets to an anti-inflammatory phenotype.\",\n      \"evidence\": \"Overexpression and siRNA in human macrophages, RT-PCR for inflammatory and cholesterol-transport genes, carotid plaque IHC\",\n      \"pmids\": [\"35662076\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism connecting LD size to inflammatory gene expression unknown\", \"Causality in vivo not established\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"In vivo kinetic study in lipodystrophy patients traced PLIN1 dysfunction to systemic consequences, showing impaired VLDL/IDL catabolism and reduced plasma LPL availability.\",\n      \"evidence\": \"Stable-isotope lipoprotein kinetics, plasma LPL mass, adipose LPL mRNA/protein in PLIN1-mutated patients\",\n      \"pmids\": [\"38899472\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanistic link between adipocyte PLIN1 loss and reduced LPL release not defined\", \"Small patient cohort\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Identifying seipin as required for PLIN1 recruitment to the droplet surface placed PLIN1 loading as a quality-control checkpoint enforcing adipocyte identity.\",\n      \"evidence\": \"BSCL2 KO in human adipocyte progenitors, differentiation, lipolysis and ceramide assays, live imaging, xenografts (preprint)\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct seipin-PLIN1 interaction vs indirect recruitment not distinguished\", \"Preprint, single lab\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Biophysical characterization defined the PLIN1 C-terminus as an intrinsically disordered region with a candidate CGI-58 binding motif, providing a structural basis for its co-regulator interactions.\",\n      \"evidence\": \"Circular dichroism, SDS-micelle conformational assays, disorder prediction and MoRF analysis on recombinant mouse C-terminal fragment\",\n      \"pmids\": [\"40109298\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No functional mutagenesis validating the EPESE motif\", \"Isolated fragment, not full-length protein in cells\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PLIN1 phosphorylation, CGI-58 release, and the disordered C-terminus mechanistically coordinate the switch from basal lipolysis suppression to stimulated lipolysis remains to be reconstituted.\",\n      \"evidence\": \"No direct timeline finding resolves the integrated phosphorylation-to-lipolysis mechanism\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural model of PLIN1 on the droplet surface bound to partners\", \"Lipase-exclusion mechanism uncharacterized at molecular resolution\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [1, 2, 7]},\n      {\"term_id\": \"GO:0008289\", \"supporting_discovery_ids\": [13]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005811\", \"supporting_discovery_ids\": [0, 12, 13]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1430728\", \"supporting_discovery_ids\": [7, 9]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CIDEC\", \"ABHD5\", \"BSCL2\", \"DLC-1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}