Affinage

PLIN5

Perilipin-5 · UniProt Q00G26

Length
463 aa
Mass
50.8 kDa
Annotated
2026-04-28
50 papers in source corpus 21 papers cited in narrative 20 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PLIN5 is a lipid droplet coat protein expressed in oxidative tissues that coordinates lipid storage, lipolysis, and mitochondrial fatty acid oxidation through regulated protein–protein interactions and signal-dependent trafficking. Under basal conditions, PLIN5 inhibits lipolysis by sequestering the ATGL co-activator CGI-58/Abhd5 on the lipid droplet surface; PKA-mediated phosphorylation at S155 releases CGI-58 to activate ATGL and simultaneously modulates lipid droplet–mitochondria contact site formation, with the phosphorylation-resistant S155A variant enhancing contacts and the phosphomimetic S155E variant reducing them (PMID:19064991, PMID:21148142, PMID:41872512). PLIN5 tethers lipid droplets to mitochondria through a C-terminal interaction with FATP4, channeling liberated fatty acids into β-oxidation, and upon lipolytic stimulation traffics monounsaturated fatty acids to the nucleus where they allosterically activate SIRT1 to drive PGC-1α/PPARα-dependent oxidative gene programs (PMID:37290445, PMID:31901447). PLIN5 expression is transcriptionally induced by PPARα and by IL-6/JAK/STAT3 signaling, and PLIN5 protein turnover is controlled by chaperone-mediated autophagy via LAMP2A (PMID:17130488, PMID:37108378, PMID:32339374).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2006 High

    Identification of PLIN5 as a PPARα-regulated lipid droplet coat protein in oxidative tissues established it as the perilipin family member linking fatty acid storage to oxidative metabolism.

    Evidence Subcellular fractionation, PPARα-knockout mice, ectopic expression, and PPAR agonist treatment across three independent labs

    PMID:16571721 PMID:17130488 PMID:17234449

    Open questions at the time
    • Mechanism by which PLIN5 simultaneously promotes TAG storage and FA oxidation was unclear
    • Domain requirements for LD targeting only partially mapped
  2. 2008 High

    Discovery that PLIN5 directly binds the ATGL co-activator CGI-58/Abhd5 revealed the molecular basis by which PLIN5 gates lipolysis at the lipid droplet surface.

    Evidence Protein interaction assays in transfected fibroblasts, in situ binding on cardiac fibers, Abhd5 E262K mutant analysis, lipolysis assays

    PMID:19064991

    Open questions at the time
    • Whether PLIN5 binds ATGL directly was not yet resolved
    • Signal that releases CGI-58 from PLIN5 was unknown
  3. 2010 High

    Demonstration that individual PLIN5 molecules bind either ATGL or CGI-58 but not both simultaneously suggested that oligomeric PLIN5 scaffolds concentrate lipolytic machinery and introduced the C-terminal domain as the ATGL-binding determinant.

    Evidence Chimeric perilipin analysis, competition experiments, and functional assays in live cells

    PMID:21148142

    Open questions at the time
    • Stoichiometry and oligomerization state of PLIN5 on LDs not defined
    • Phosphorylation-dependent switch not yet shown
  4. 2012 Medium

    Hepatocyte loss-of-function studies confirmed that PLIN5 acts as a lipolysis brake, with knockdown increasing ATGL-dependent lipolysis and β-oxidation.

    Evidence siRNA knockdown and overexpression in AML12/primary hepatocytes, lipolysis and oxidation measurements

    PMID:22675471

    Open questions at the time
    • Phosphorylation site mediating lipolysis activation not identified
    • Relationship between LD-association domain and lipolysis-inhibitory function was correlative
  5. 2014 Medium

    Detection of PLIN5 in the mitochondrial fraction of skeletal muscle, increasing with contraction, provided the first evidence that PLIN5 physically associates with mitochondria to facilitate FA channeling during exercise.

    Evidence Differential centrifugation and Western blotting from rat skeletal muscle after contraction

    PMID:25318747

    Open questions at the time
    • Mitochondrial binding partner not identified
    • Could not distinguish LD-mitochondria contact sites from free mitochondrial PLIN5
  6. 2019 High

    The discovery that PLIN5 binds monounsaturated fatty acids and upon PKA stimulation carries them to the nucleus to allosterically activate SIRT1/PGC-1α established a lipid signaling relay from LDs to transcriptional control of oxidative metabolism.

    Evidence FA binding assays, nuclear fractionation, in vitro SIRT1 activation assay, animal model validation

    PMID:31901447

    Open questions at the time
    • Structural basis of FA binding by PLIN5 unknown
    • Whether nuclear PLIN5 has additional transcriptional targets beyond PGC-1α/PPARα not explored
  7. 2020 Medium

    Identification of PLIN5 as a chaperone-mediated autophagy substrate degraded via LAMP2A revealed how PLIN5 protein turnover is coupled to lipid droplet breakdown in hepatocytes.

    Evidence Liver-specific LAMP2A-KO mice and LAMP2A-deficient HepG2 cells with LD accumulation phenotype

    PMID:32339374

    Open questions at the time
    • CMA-targeting motif on PLIN5 not mapped
    • Interplay between CMA-mediated PLIN5 degradation and PKA-mediated PLIN5 phosphorylation not addressed
  8. 2020 Medium

    Plin5-knockout cardiomyocytes confirmed that PLIN5 restrains ATGL activity in the heart, as pharmacological ATGL inhibition fully rescued LD depletion in Plin5−/− cells.

    Evidence Isolated adult cardiomyocytes from Plin5-KO mice, ATGL inhibitor rescue, LD quantification

    PMID:33373698

    Open questions at the time
    • Heart-specific consequences of chronic PLIN5 loss on mitochondrial function not fully delineated
    • Phosphorylation-dependent regulation not tested in this system
  9. 2022 Medium

    The PKA-phosphorylation model was consolidated: basal PLIN5 sequesters CGI-58 to suppress lipolysis, and phosphorylation releases CGI-58 to activate ATGL, providing a unified regulatory switch.

    Evidence Review synthesis of cell-based phosphorylation and protein interaction studies

    PMID:35401929

    Open questions at the time
    • Specific phosphorylation site(s) responsible had not been mutagenized in vivo
    • Whether additional kinases target PLIN5 was unresolved
  10. 2023 High

    Identification of FATP4 as the mitochondrial binding partner of PLIN5 at LD–mitochondria contact sites, with phosphorylation promoting FA transfer to β-oxidation, provided the molecular tether linking lipolysis to mitochondrial oxidation.

    Evidence Co-IP, proximity ligation assay, domain mapping with minimal constructs, phospho-mutant β-oxidation assays in starved myoblasts

    PMID:37290445

    Open questions at the time
    • Structure of the PLIN5–FATP4 complex not resolved
    • Whether PLIN5 also tethers to ER or other organelles via distinct partners unclear
  11. 2023 High

    Discovery of a PLIN5–SERCA2 interaction in cardiomyocytes, enhancing Ca²⁺ cycling and contractility, expanded PLIN5 function beyond lipid metabolism to excitation-contraction coupling.

    Evidence Quantitative proteomics, proximity ligation assay, live Ca²⁺ imaging in cardiac-specific PLIN5-transgenic mice

    PMID:36717246

    Open questions at the time
    • Direct binding domain on PLIN5 for SERCA2 not mapped
    • Whether this reflects a lipid-dependent or lipid-independent mechanism is unknown
  12. 2025 Medium

    In vitro reconstitution demonstrated that PLIN5 directly mediates stable attachment of lipid droplet monolayers to bilayer membranes without promoting fusion, establishing an intrinsic membrane-tethering activity.

    Evidence Reconstituted artificial LDs coated with PLIN5, LUV bilayers, dual fluorescence to distinguish tethering from fusion

    PMID:41459334

    Open questions at the time
    • Physiological relevance to specific organelle contacts not demonstrated in this system
    • Minimal tethering domain not identified
  13. 2026 High

    Phosphosite-resolution mutagenesis in vivo demonstrated that S155 is the key PKA site controlling LD–mitochondria contact dynamics and hepatic lipid flux: S155A enhances contacts and LD expansion while S155E reduces them, resolving the phosphoswitch to a single residue.

    Evidence Single-cell tissue imaging, spatial proteomics, PLIN5 S155A/S155E/WT overexpression in Western-diet-fed mice

    PMID:41872512

    Open questions at the time
    • Whether S155 phosphorylation also controls CGI-58 release and nuclear translocation in the same hepatic system was not directly tested
    • Potential additional phosphorylation sites contributing to PLIN5 regulation not ruled out

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis of PLIN5 interactions (with CGI-58, ATGL, FATP4, and SERCA2), the full phosphorylation code governing distinct PLIN5 outputs (lipolysis, tethering, nuclear translocation), and whether the SERCA2-mediated Ca²⁺ function is lipid-dependent.
  • No atomic-resolution structure of PLIN5 or any of its complexes
  • Integrated phosphorylation-dependent regulation of lipolysis vs. tethering vs. nuclear signaling not tested in a single system
  • Physiological relevance of PLIN5–SERCA2 interaction to cardiac lipotoxicity models not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0008289 lipid binding 2 GO:0060090 molecular adaptor activity 2
Localization
GO:0005811 lipid droplet 5 GO:0005634 nucleus 2 GO:0005739 mitochondrion 2
Pathway
R-HSA-1430728 Metabolism 6 R-HSA-162582 Signal Transduction 4 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-9612973 Autophagy 1
Partners
ABHD5FATP4HSD17B11PGC1APNPLA2SERCA2SIRT1TBC1D15

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 PLIN5 (OXPAT/MLDP/LSDP5) localizes to the surface of lipid droplets in oxidative tissues and its expression is induced by PPARα activation (fasting, insulin deficiency, PPARα agonists). Ectopic expression promotes fatty acid-induced triacylglycerol accumulation and long-chain fatty acid oxidation. Subcellular fractionation, ectopic expression in cells, GFP-fusion live imaging, PPARα knockout mice, pharmacological PPAR agonist treatment Diabetes / Journal of Biological Chemistry / Biochimica et biophysica acta High 16571721 17130488 17234449
2006 The N-terminal PAT-1 domain plus a following 33-mer domain of PLIN5 (MLDP) is required for targeting to lipid droplet surfaces, as shown by deletion analysis. Deletion mutagenesis with GFP-fusion protein localization in cells The Journal of biological chemistry Medium 16571721
2008 PLIN5 (Mldp/LSDP5) directly binds Abhd5 (CGI-58, the protein activator of ATGL) on lipid droplet surfaces; this interaction is dynamic, increases with oleic acid treatment, and is required for efficient ATGL-mediated lipolysis at PLIN5-containing lipid droplets. Protein-protein interaction assay in transfected fibroblasts, in situ binding on microdissected cardiac muscle fibers, Abhd5 E262K mutant with impaired Mldp binding, cellular lipolysis assays The Journal of biological chemistry High 19064991
2010 PLIN5 interacts with both ATGL and its activator Abhd5, but individual PLIN5 molecules bind either ATGL or Abhd5 but not both simultaneously, suggesting oligomeric complexes concentrate these proteins at lipid droplet surfaces. The C-terminal 64 amino acids of PLIN5 (residues 200–463) are necessary and sufficient for differential binding of ATGL to PLIN5 (but not PLIN1). Protein interaction assays in live cells, in situ binding, chimeric/mutant perilipin analysis, competition experiments, neutral lipid accumulation assays The Journal of biological chemistry High 21148142
2012 PLIN5 (LSDP5) inhibits lipolysis and fatty acid β-oxidation in hepatocytes; knockdown stimulates lipolysis and increases PPARα expression and mitochondrial β-oxidation. The lipid droplet-targeting and clustering domain maps to the N-terminal 188 amino acids. Overexpression and siRNA knockdown in AML12 hepatocytes and primary hepatocytes, serial deletion analysis, triglyceride content measurement, lipolysis assay, mitochondrial oxidation measurement PloS one Medium 22675471
2014 PLIN5 is found in the mitochondrial fraction of skeletal muscle, and its mitochondrial content increases ~1.6-fold following muscle contraction, consistent with a role in facilitating mitochondrial fatty acid oxidation during lipolysis. Mitochondrial isolation by differential centrifugation from rat red gastrocnemius, Western blotting, immunofluorescence Physiological reports Medium 25318747
2019 PLIN5 is a fatty-acid-binding protein that preferentially binds lipid droplet-derived monounsaturated fatty acids (MUFAs) and, following cAMP/PKA-mediated lipolytic stimulation, traffics them to the nucleus where MUFAs allosterically activate SIRT1 toward PGC-1α, thereby enhancing PGC-1α/PPARα signaling and oxidative metabolism. Fatty acid binding assay, cAMP/PKA stimulation, nuclear fractionation, SIRT1 allosteric activation assay with defined substrates, cell and animal model experiments with SIRT1-dependent pathway validation Molecular cell High 31901447
2020 PLIN5 is a substrate of chaperone-mediated autophagy (CMA); its degradation via LAMP2A is required for lipid droplet breakdown in hepatocytes. Disruption of CMA (LAMP2A deletion) stabilizes PLIN5, obstructs LD breakdown, and causes lipid homeostasis imbalance. Liver-specific LAMP2A-knockout mice, LAMP2A-deficient HepG2 cells, co-localization studies, lipid droplet accumulation assays Liver international Medium 32339374
2023 PLIN5 interacts with the acyl-CoA synthetase FATP4 (ACSVL4) on mitochondria at lipid droplet-mitochondria contact sites; the C-terminal domains of PLIN5 and FATP4 constitute a minimal interaction capable of inducing organelle contacts. Phosphorylation of PLIN5 promotes LD-to-mitochondria fatty acid transfer and β-oxidation during starvation, and an intact PLIN5 mitochondrial tethering domain is required. Co-immunoprecipitation, proximity ligation assay, domain mapping with minimal constructs, phosphorylation-deficient/mimetic mutants, β-oxidation assays in starved myoblasts, human and murine cell models Developmental cell High 37290445
2023 PLIN5 interacts with SERCA2 (sarcoplasmic/endoplasmic reticulum Ca2+ ATPase 2) in cardiomyocytes; cardiac-specific overexpression of PLIN5 increases intracellular Ca2+ release during contraction and Ca2+ removal during relaxation, enhancing SERCA2 function and cardiomyocyte contractility. Quantitative proteomics of PLIN5-overexpressing hearts, in situ proximity ligation assay, live imaging of Ca2+ dynamics, cardiac-specific transgenic mice (MHC-Plin5) Life science alliance High 36717246
2022 Under basal (non-phosphorylated) conditions, PLIN5 inhibits lipolysis by sequestering CGI-58 (Abhd5), preventing it from activating ATGL. Upon PKA-mediated phosphorylation of PLIN5 (e.g., during fasting, cold, or exercise), PLIN5 releases CGI-58, which then binds and activates ATGL, accelerating lipolysis. Review synthesizing cell-based phosphorylation experiments and protein interaction studies Oxidative medicine and cellular longevity Medium 35401929
2022 PLIN5 interacts with PGC-1α in vascular smooth muscle cells; Plin5 knockdown reduces Plin5-PGC-1α interaction, increases ROS, and promotes VSMC proliferation and migration. PGC-1α overexpression rescues ROS elevation and VSMC dysfunction in Plin5-deficient cells. Co-immunoprecipitation, wire-injury mouse model, Plin5 knockdown mice (Plin5±), ROS measurement, proliferation/migration assays, PGC-1α overexpression rescue Bioengineered Medium 35470759
2025 HSD17β11 facilitates the interaction between PLIN5 and ATGL on lipid droplets, enabling efficient PKA-stimulated lipolysis; HSD17β11 deletion impairs this PLIN5-ATGL interaction and reduces lipolysis in human cell lines. HSD17β11 deletion in human cell lines, lipolysis assays, co-immunoprecipitation of PLIN5 and ATGL, PKA stimulation Journal of lipid research Medium 41238190
2025 TBC1D15 is recruited to mitochondrial membranes in hepatocytes upon alcohol exposure and interacts with PLIN5 through its 10-180 aa domain, promoting mitochondria-lipid droplet contacts and PKA-induced nuclear translocation of PLIN5. Hepatocyte-specific TBC1D15 overexpression mice, co-immunoprecipitation domain mapping, immunofluorescence of PLIN5 nuclear translocation, PKA inhibition experiments Metabolism: clinical and experimental Medium 40334909
2026 PLIN5 phosphorylation at S155 regulates mitochondria-lipid droplet contact formation and hepatic lipid flux: the phosphorylation-resistant S155A variant enhances organelle contacts and LD expansion, while the phosphomimetic S155E variant reduces contacts and yields fewer, smaller LDs. PLIN5 overexpression in Western-diet-fed mice reduces lipotoxicity. Single-cell tissue imaging (scPhenomics), spatial proteomics, PLIN5 phosphorylation variant overexpression (S155A, S155E, WT) in mice, LD/mitochondria contact quantification, lipid content measurement Nature metabolism High 41872512
2020 Isolated Plin5-deficient cardiomyocytes store fewer lipid droplets than wild-type, primarily because PLIN5 represses ATGL lipase activity; inhibiting ATGL activity normalizes LD levels in Plin5-/- cardiomyocytes to wild-type levels. Isolated adult cardiomyocytes from Plin5+/+ and Plin5-/- mice, ATGL inhibitor treatment, fatty acid oxidation assays, lipid droplet quantification Biochimica et biophysica acta. Molecular and cell biology of lipids Medium 33373698
2025 PLIN5 regulates lipid metabolism and mitochondrial dynamics in pancreatic β-cells via PGC-1α/Drp1 signaling: PLIN5 knockdown decreases PGC-1α and increases Drp1, causing mitochondrial dysfunction, while PLIN5 overexpression reverses high-glucose-induced damage. PLIN5 also influences PGC-1α binding to the Drp1 promoter. siRNA knockdown and lentiviral overexpression in INS-1 cells, db/db mice, Western blotting, qPCR, immunofluorescence, chromatin-related promoter binding assay Endocrine Medium 40884681
2023 PLIN5 expression in liver (Hep3B cells) is induced by IL-6 in a dose- and time-dependent manner through the JAK/STAT3 signaling pathway; this induction can be blocked by TGF-β and TNF-α, and is modulated by IL-6 trans-signaling. IL-6 treatment of Hep3B cells, JAK/STAT3 inhibitors, TGF-β and TNF-α co-treatment, soluble IL-6R addition, quantitative protein and mRNA analysis International journal of molecular sciences Medium 37108378
2025 In an in vitro reconstitution system, PLIN5 promotes stable attachment of lipid droplet monolayers to bilayer membranes (LUVs) while preventing membrane fusion, demonstrating a direct physical role of PLIN5 in mediating organelle contact sites. In vitro reconstitution with artificial LDs coated with PLIN5, large unilamellar vesicles (LUVs), dual fluorescence labeling to distinguish fusion from stable attachment Biochemistry and biophysics reports Medium 41459334
2021 Leptin promotes FTO-mediated demethylation (reduction in m6A methylation) of Plin5 mRNA, increasing Plin5 protein expression in adipose tissue, which in turn reduces lipid droplet size and promotes triglyceride metabolism. In vivo leptin treatment of piglets, in vitro porcine adipocyte FTO overexpression/interference, m6A methylation measurement, Plin5 overexpression functional assays International journal of molecular sciences Low 34638947

Source papers

Stage 0 corpus · 50 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 OXPAT/PAT-1 is a PPAR-induced lipid droplet protein that promotes fatty acid utilization. Diabetes 268 17130488
2006 LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing tissues. Biochimica et biophysica acta 203 17234449
2010 Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase. The Journal of biological chemistry 186 21148142
2006 MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha. The Journal of biological chemistry 179 16571721
2019 Lipid Droplet-Derived Monounsaturated Fatty Acids Traffic via PLIN5 to Allosterically Activate SIRT1. Molecular cell 134 31901447
2008 Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation. The Journal of biological chemistry 122 19064991
2023 PLIN5 interacts with FATP4 at membrane contact sites to promote lipid droplet-to-mitochondria fatty acid transport. Developmental cell 105 37290445
2009 Adipocyte differentiation-related protein and OXPAT in rat and human skeletal muscle: involvement in lipid accumulation and type 2 diabetes mellitus. The Journal of clinical endocrinology and metabolism 83 19602560
2013 Inactivation of Plin4 downregulates Plin5 and reduces cardiac lipid accumulation in mice. American journal of physiology. Endocrinology and metabolism 82 23423172
2017 Plin5 alleviates myocardial ischaemia/reperfusion injury by reducing oxidative stress through inhibiting the lipolysis of lipid droplets. Scientific reports 78 28218306
2015 Unraveling the roles of PLIN5: linking cell biology to physiology. Trends in endocrinology and metabolism: TEM 72 25682370
2020 Disruption of Plin5 degradation by CMA causes lipid homeostasis imbalance in NAFLD. Liver international : official journal of the International Association for the Study of the Liver 55 32339374
2014 Lipocalin-2 (LCN2) regulates PLIN5 expression and intracellular lipid droplet formation in the liver. Biochimica et biophysica acta 49 25086218
2012 LSDP5 enhances triglyceride storage in hepatocytes by influencing lipolysis and fatty acid β-oxidation of lipid droplets. PloS one 44 22675471
2016 Decoration of intramyocellular lipid droplets with PLIN5 modulates fasting-induced insulin resistance and lipotoxicity in humans. Diabetologia 41 26864436
2022 Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues. Oxidative medicine and cellular longevity 39 35401929
2019 Targeting PLIN2/PLIN5-PPARγ: Sulforaphane Disturbs the Maturation of Lipid Droplets. Molecular nutrition & food research 30 31325205
2019 MicroRNA-370 protects against myocardial ischemia/reperfusion injury in mice following sevoflurane anesthetic preconditioning through PLIN5-dependent PPAR signaling pathway. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 28 30856533
2011 Subcellular localization of skeletal muscle lipid droplets and PLIN family proteins OXPAT and ADRP at rest and following contraction in rat soleus muscle. American journal of physiology. Regulatory, integrative and comparative physiology 28 22012700
2022 Plin5, a New Target in Diabetic Cardiomyopathy. Oxidative medicine and cellular longevity 22 35509833
2014 Higher PLIN5 but not PLIN3 content in isolated skeletal muscle mitochondria following acute in vivo contraction in rat hindlimb. Physiological reports 18 25318747
2021 Leptin Reduces Plin5 m6A Methylation through FTO to Regulate Lipolysis in Piglets. International journal of molecular sciences 16 34638947
2022 Plin5 inhibits proliferation and migration of vascular smooth muscle cell through interacting with PGC-1α following vascular injury. Bioengineered 15 35470759
2020 Isolated Plin5-deficient cardiomyocytes store less lipid droplets than normal, but without increased sensitivity to hypoxia. Biochimica et biophysica acta. Molecular and cell biology of lipids 12 33373698
2019 Plin5/p-Plin5 Guards Diabetic CMECs by Regulating FFAs Metabolism Bidirectionally. Oxidative medicine and cellular longevity 12 31772713
2023 Cardiac Plin5 interacts with SERCA2 and promotes calcium handling and cardiomyocyte contractility. Life science alliance 11 36717246
2021 Dapagliflozin Mediates Plin5/PPARα Signaling Axis to Attenuate Cardiac Hypertrophy. Frontiers in pharmacology 11 34630108
2017 Plin5 deficiency promotes atherosclerosis progression through accelerating inflammation, apoptosis and oxidative stress. Journal of cellular biochemistry 9 29215758
2024 PLIN5 Suppresses Lipotoxicity and Ferroptosis in Cardiomyocyte via Modulating PIR/NF-κB Axis. International heart journal 8 38749744
2020 Methylation of PLIN5 is a crucial biomarker and is involved in ovarian cancer development. Translational cancer research 8 35117648
2025 TBC1D15 protects alcohol-induced liver injury in female mice through PLIN5-mediated mitochondrial and lipid droplet contacting. Metabolism: clinical and experimental 7 40334909
2023 Lipid-Independent Regulation of PLIN5 via IL-6 through the JAK/STAT3 Axis in Hep3B Cells. International journal of molecular sciences 7 37108378
2022 Hepatic PLIN5 Deficiency Impairs Lipogenesis through Mitochondrial Dysfunction. International journal of molecular sciences 7 36555245
2021 Role of Plin5 Deficiency in Progression of Non-Alcoholic Fatty Liver Disease Induced by a High-Fat Diet in Mice. Journal of comparative pathology 7 34886991
2020 Involvement of activation of PLIN5-Sirt1 axis in protective effect of glycycoumarin on hepatic lipotoxicity. Biochemical and biophysical research communications 7 32448510
2020 EPA/DHA Concentrate by Urea Complexation Decreases Hyperinsulinemia and Increases Plin5 in the Liver of Mice Fed a High-Fat Diet. Molecules (Basel, Switzerland) 7 32698439
2024 PLIN5 contributes to lipophagy of hepatic stellate cells induced by inorganic arsenic. Ecotoxicology and environmental safety 4 39700776
2025 Plin5: A potential therapeutic target for type 2 diabetes mellitus. Diabetology & metabolic syndrome 3 40176076
2026 PLIN5 phosphorylation orchestrates mitochondria lipid-droplet coupling to control hepatic lipid flux and steatosis. Nature metabolism 1 41872512
2025 PLIN5 regulates lipid metabolism via PGC-1α/Drp1 signaling in islet β-cells. Endocrine 1 40884681
2024 Differential Plin5 response to high-fat diet in cardiomyocytes isolated from young and aged mice. Mechanisms of ageing and development 1 39510385
2010 [Construction of eukaryotic fusion expression vectors of LSDP5 and cellular localization]. Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology 1 20423650
2026 Acute deletion of PLIN5 in brown adipocytes causes mitochondrial dysfunction and cold intolerance. bioRxiv : the preprint server for biology 0 41509390
2026 KIF13B Attenuates Sepsis-Induced Myocardial Dysfunction through the Stabilization of PLIN5. Research (Washington, D.C.) 0 41531892
2026 MLDP-AS: an optimized next-generation sequencing assay for enhanced detection of technically challenging variants in expanded carrier screening. Journal of translational medicine 0 41691275
2025 PLIN5 deficiency ameliorates metabolic dysfunction‑associated fatty liver disease by inhibiting ferroptosis. Molecular medicine reports 0 41104863
2025 PLIN5 affects the fibrosis and progression of pancreatic cancer via modulation of pancreatic stellate cells. Life sciences 0 41187900
2025 HSD17β11 regulates PLIN5-ATGL mediated lipolysis, but not hepatic lipid metabolism in mice. Journal of lipid research 0 41238190
2025 PLIN5 Promotes Lipid Reconstitution in Goat Intramuscular Fat via the PPARγ Signaling Pathway. Biology 0 41300337
2025 Influence of PLIN5 and lipid composition on lipid droplet contact sites with other organelles. Biochemistry and biophysics reports 0 41459334