{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPerilipin‐3 (PLIN3), formerly known as TIP47, is an evolutionarily conserved lipid droplet–associated protein that plays a central role in the biogenesis and regulation of neutral lipid storage. Structural and biochemical studies reveal that PLIN3 employs an amino‐terminal PAT domain together with 11‐mer repeat regions that fold into amphipathic helices to mediate its reversible association with the unique phospholipid monolayer of lipid droplets. Specific residues—such as a conserved glutamate—mediate high‐affinity binding to diacylglycerol (DAG), a key precursor in triacylglycerol synthesis, thereby promoting droplet formation and modulating lipid deposition and mobilization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nInvestigations in a variety of cell types have underscored PLIN3’s pivotal role in regulating intracellular lipid metabolism. In human skeletal muscle, increased PLIN3 following lipolytic stimulation correlates with enhanced fatty acid oxidation, while studies in macrophages, neutrophils, and sebocytes have demonstrated its critical function in lipid droplet maturation and neutral lipid accumulation. Moreover, in lactating breast tissue, PLIN3 is a prominent constituent of milk fat globule membranes, with its levels showing strong associations with milk lipid content."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its role in lipid storage, PLIN3 modulates retinoid metabolism in epithelial cells by inhibiting retinyl ester hydrolysis—a function that contributes to the regulation of retinoic acid biosynthesis and, consequently, proper cell differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPLIN3 also exerts multifaceted functions in viral pathogenesis. For HIV‐1, PLIN3 is essential for the incorporation of envelope glycoproteins into budding virions through its ability to form complexes with viral structural proteins. In hepatitis C virus (HCV) infection, PLIN3 interacts with nonstructural proteins such as NS5A to facilitate the targeting of the viral RNA genome to lipid droplets, thus promoting efficient genome replication and particle assembly. In parallel, PLIN3 has been implicated in the envelopment of vaccinia virus and—even acting oppositely as a restriction factor—in Sendai virus, where it modulates viral protein synthesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nApart from its canonical role at the lipid droplet surface, PLIN3 functions as an effector in endosomal trafficking. Its interaction with specific Rab GTPases is critical for establishing and maintaining key membrane compartments involved in vesicular transport, thereby linking lipid storage with broader aspects of cellular membrane dynamics."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of PLIN3 is also implicated in metabolic and endocrine disorders. In adipose tissue, altered expression of PLIN3 has been associated with conditions such as polycystic ovary syndrome, underscoring its contribution to intracellular lipid handling and systemic metabolic control."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging evidence indicates that abnormal PLIN3 expression is common in various cancers, including renal cell carcinoma, prostate cancer, lung adenocarcinoma, gastric cancer, and oral squamous cell carcinoma. In these malignant contexts, altered PLIN3 levels are linked to changes in lipophagy, autophagic flux, and chemotherapeutic responses, suggesting that PLIN3 may serve as both a biomarker for tumor progression and a potential target for therapeutic intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, PLIN3 exhibits cytoprotective functions by stabilizing mitochondrial membranes under conditions of oxidative stress, thereby preventing mitochondrial depolarization and ensuing cell death. This protective role further highlights the multifaceted contributions of PLIN3 to cell survival and metabolic integrity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shinji Miura, Jai-Wei Gan, Joseph Brzostowski, et al. 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