{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPNPLA2, which encodes adipose triglyceride lipase (ATGL), is the key enzyme initiating triglyceride hydrolysis by catalyzing the release of the first fatty acid from stored triglycerides. ATGL is highly expressed in adipose tissue and lipid‐storing cells, where it localizes to lipid droplets and displays substrate specificity toward triacylglycerols. Its catalytic efficiency and proper subcellular localization rely on a conserved patatin domain, and full enzymatic activity requires interaction with the coactivator CGI-58. These features underpin its central role in mobilizing fatty acids for energy production in both adipose and nonadipose tissues, with additional participation in maintaining lipid and energy homeostasis."}, {"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": "\nBeyond its core lipolytic function, ATGL is subject to intricate regulation by protein–protein interactions and posttranslational modifications. It is modulated by binding partners such as CGI-58, several perilipin proteins, and UBXD8, which together orchestrate its recruitment to lipid droplets and adjust its activity in response to metabolic cues. Dysfunctions or mutations in PNPLA2 that affect the catalytic domain or lipid droplet binding—often impacting the C-terminal regions—result in defective triglyceride breakdown and cause neutral lipid storage diseases (with or without myopathy) and contribute to pathological states such as cachexia and insulin resistance. Furthermore, studies in human adipocytes and muscle reveal that ATGL expression and activity are tightly linked to adipocyte size, intracellular fatty acid levels, and overall metabolic health."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNew insights have further broadened the functional repertoire of PNPLA2/ATGL. In addition to its classical lipase activity, ATGL has been implicated in biosynthetic transacylation reactions that generate bioactive lipids, such as FAHFAs, expanding its role into cell signaling and metabolic regulation. ATGL also appears to function as part of receptor complexes (for example, mediating pigment epithelium‐derived factor signaling) and has been associated with tumor suppressor activities in several cancers. Transcriptional regulation—mediated by factors like Egr1 and HuR—and feedback inhibition by long-chain acyl-CoAs underscore the enzyme’s sensitivity to intracellular metabolic status and its involvement in conditions ranging from obesity to cancer. These diverse regulatory inputs and interactions highlight ATGL’s pivotal role in coordinating lipid mobilization, energy homeostasis, and cellular signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Robert Zimmermann, Juliane G Strauss, Guenter Haemmerle, et al. 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