ArticleScientific reports2016
Perilipin2 plays a positive role in adipocytes during lipolysis by escaping proteasomal degradation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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58 citing papers in PubMed, 102 citations in OpenAlex.
- Lipid droplets as redox-active organelles after spinal cord injury: lipid peroxidation, mitochondrial dysfunction, and neuroinflammation.Redox report : communications in free radical research · 2026Review
- Differences of PPARD Expression in the Liver of Cattle with Different Marbling Grades.Animals : an open access journal from MDPI · 2026Article
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- Transcriptomic Exploration of Muscle Development and Fat Deposition Trait Diversity in Selected Indian Sheep Breeds: Implications for Meat Quality and Yield.Animals : an open access journal from MDPI · 2026Article
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- The role of lipid metabolism and peroxisome proliferator activation in mediating pro-cancer phenotypes of poly- and perfluoroalkyl substances in testicular cancer.Environmental toxicology and pharmacology · 2025Article
- "Seipin mediates Perilipin-1 recruitment to lipid droplets to preserve human adipocyte identity".bioRxiv : the preprint server for biology · 2025Article
- Perilipins: key targets for regulating lipid metabolism and alleviating abnormal lipid metabolism through exercise.Diabetology & metabolic syndrome · 2025Review
- Nanomedicine targeting PPAR in adipose tissue macrophages improves lipid metabolism and obesity-induced metabolic dysfunction.Science advances · 2025Article
- Essential Biology of Lipid Droplets.Annual review of biochemistry · 2025Review
- Article
- CSN-CRL Complexes: New Regulators of Adipogenesis.Biomolecules · 2025Review
- Omics Approaches to Study Perilipins and Their Significant Biological Role in Cardiometabolic Disorders.International journal of molecular sciences · 2025Review
- PLINs-mediated organelle interactions: a key of exercise-mediated improvement of skeletal muscle lipid metabolism disorders.Frontiers in endocrinology · 2025Review
- Comprehensive Analysis of DGATs and PLINs in Ovarian Cancer: Implications for Diagnosis and Prognosis.BioMed research international · 2025Article
- Fibro-adipogenic progenitor cells in skeletal muscle unloading: metabolic and functional impairments.Skeletal muscle · 2024Article
- Protein posttranslational modifications in metabolic diseases: basic concepts and targeted therapies.MedComm · 2024Review
- Fatty acid profiles unveiled: gene expression in Yanbian yellow cattle adipose tissues offers new insights into lipid metabolism.Archives animal breeding · 2024Article
- Perilipin2 inhibits the replication of hepatitis B virus deoxyribonucleic acid by regulating autophagy under high-fat conditions.World journal of virology · 2023Article
- Chaperone-mediated autophagy regulates adipocyte differentiation.Science advances · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Perilipin2 (Plin2), also known as adipose differentiation-related protein (ADRP), or adipophilin, is a member of the PAT family involved in lipid droplet (LD) formation in the liver and peripheral tissues. Although Plin2 was originally identified as a highly expressed gene in adipocytes, its physiological role in mature adipocytes is largely unknown. In this report, we investigated the regulation of Plin2 expression and its function in differentiated adipocytes of mouse embryonic fibroblasts (MEFs). Plin2 mRNA levels increased during adipocyte differentiation whereas protein levels did not. Plin2 was degraded through the ubiquitin-proteasome pathway but was inhibited by lipolytic inducers. Furthermore, lentiviral-mediated Plin2 knockdown attenuated lipolysis in differentiated MEFs in a time-dependent manner. Oleic acid-induced LD formation enhanced Plin2 protein stability when it was localized to LDs. Furthermore, a mutational analysis revealed that the ubiquitination and degradation of Plin2 required both the second and third alanine in the N-terminal region. These results suggest that Plin2 is degraded in the cytosol in its N-terminal amino acid sequence-dependent manner and instead becomes stable when localized on LDs. Our findings highlight the relationship between protein stability and a previously unnoticed function of Plin2 during lipolysis in adipocytes.
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