{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPerilipin 1 (PLIN1) is a pivotal adipocyte‐specific protein that coats intracellular lipid droplets and orchestrates the balance between lipid storage and mobilization. In the basal state, unphosphorylated PLIN1 protects stored triglycerides by forming a physical barrier that limits access of lipases; upon hormonal stimulation, however, specific phosphorylation events induce structural rearrangements that facilitate the recruitment of lipolytic enzymes (such as hormone‐sensitive lipase) to the droplet surface, thereby enhancing triglyceride hydrolysis and energy mobilization. This dynamic regulation of lipolysis is tightly controlled at both the transcriptional and post‐translational levels, and is fundamental to maintaining whole‐body energy homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its essential role in adipocytes, PLIN1 exhibits diverse functions in several tissues that impact metabolic health. Its de novo expression in steatotic hepatocytes, for instance, implicates PLIN1 in the development of nonalcoholic fatty liver disease, whereas in pancreatic β‐cells its capacity to sequester lipids protects against lipotoxicity and preserves glucose‐stimulated insulin secretion. In addition, PLIN1 is found in macrophage foam cells, where altered lipid droplet dynamics contribute to atherosclerotic plaque formation. Such tissue‐specific regulation is achieved in part through modulation by nuclear receptors and epigenetic mechanisms, which together fine‐tune PLIN1 expression and, consequently, systemic energy balance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic variations and advanced regulatory insights further underscore the clinical importance of PLIN1. Frameshift mutations and common single nucleotide polymorphisms at the PLIN1 locus are linked to a spectrum of metabolic disturbances—including familial partial lipodystrophy, severe insulin resistance and dyslipidemia, as well as variable obesity risk and altered responses to dietary interventions and pharmacotherapy. Complementary structural studies have revealed that conserved amphipathic domains within perilipin 1 are crucial for its precise targeting to the lipid droplet surface and for establishing microdomains that regulate lipase access. Collectively, these multifaceted findings illustrate how genetic, epigenetic, and post‐translational mechanisms converge to finely regulate PLIN1 function, ultimately impacting lipid storage, mobilization, and systemic metabolic homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "45"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "S Mottagui-Tabar, M Rydén, P Löfgren, et al. 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