{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPerilipin 2 (PLIN2), also known as adipophilin or adipose differentiation‐related protein, is a key lipid droplet–associated protein that governs intracellular lipid homeostasis across diverse cell types. Much work has demonstrated that PLIN2 coats newly formed lipid droplets, facilitates their biogenesis and stabilization, and modulates lipid storage in response to metabolic cues. Early studies in adipocyte‐ and liver‐derived cells indicated that PLIN2 expression increases during fatty acid loading, fasting, or hypoxic stress, thereby promoting triglyceride accumulation and protecting cells from lipotoxicity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn metabolic tissues such as liver and skeletal muscle, PLIN2 plays a dual role. In models of nonalcoholic fatty liver disease and in hepatocyte‐like cells derived from pluripotent stem cells, increased PLIN2 expression is linked to enhanced lipid droplet accumulation and alterations in metabolic gene networks—often in conjunction with perturbations in peroxisome proliferator–activated receptor (PPAR) signaling—while interference with its expression can markedly alter lipid, glucose, and purine metabolism. In skeletal muscle, PLIN2 colocalizes with intramyocellular lipid droplets and its association appears modulated during exercise, with preferential consumption of PLIN2‐coated droplets contributing to fuel mobilization. In addition, altered PLIN2 levels may trigger inflammatory cascades and impair insulin signaling in myoblasts, underscoring its relevance in insulin resistance and foam cell formation in atherosclerosis, as well as its emerging diagnostic value in clear‐cell renal carcinoma."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional regulatory layers ensure that PLIN2 levels are tailored to cellular lipid needs. The unbound, cytosolic form of PLIN2 is subject to ubiquitin‐proteasome–mediated degradation—via mechanisms involving the Ac/N‑end rule and the E3 ligase TEB4—thus permitting dynamic adjustment of lipid droplet content. Moreover, in placental trophoblasts hypoxia‐stimulated upregulation of PLIN2 appears to be a protective adaptation to minimize cell death while potentially modulating nutrient transport. Collectively, these findings link PLIN2 not only to the assembly, stabilization, and selective utilization of lipid droplets but also to broader metabolic and inflammatory signaling networks with implications for conditions ranging from obesity and insulin resistance to cancer and atherosclerosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sirkku T Saarikoski, Steven P Rivera, Oliver Hankinson "}, {"type": "b", "children": [{"type": "t", "text": "Mitogen-inducible gene 6 (MIG-6), adipophilin and tuftelin are inducible by hypoxia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0014-5793(02)03475-0"}], "href": "https://doi.org/10.1016/s0014-5793(02"}, {"type": "t", "text": "03475-0) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12387890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12387890"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Paul Targett-Adams, Doreen Chambers, Sarah Gledhill, et al. 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