{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPLA2G6 encodes the group VIA calcium‐independent phospholipase A₂β enzyme, which catalyzes the hydrolysis of membrane glycerophospholipids at the sn‑2 position to release free fatty acids and lysophospholipids. Such lipid mediators are essential for membrane remodeling, phospholipid turnover, and the generation of bioactive species that modulate energy storage and signaling. For example, studies in adipocytes have shown that PLA2G6 family members not only display triacylglycerol lipase and acylglycerol transacylase activities but also contribute to phospholipid remodeling in a manner that can regulate cellular lipid composition and even influence the activation of thermosensitive channels in tissues such as the prostate."}, {"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": "\nDysfunction of PLA2G6 has been strongly linked to a spectrum of neurodegenerative disorders. Mutations in its gene are the cause of infantile neuroaxonal dystrophy (INAD), neurodegeneration with brain iron accumulation (NBIA), and early‐onset dystonia‐parkinsonism, among others. The enzyme’s impaired phospholipid hydrolysis disrupts membrane homeostasis, promotes mitochondrial abnormalities and lipid peroxidation, and leads to the aberrant accumulation of toxic lipid species—all of which contribute to neuronal degeneration, tau and α‑synuclein pathology, and parkinsonian features. Genetic screens and pathological examinations across diverse patient cohorts have underscored its central role in these disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in membrane remodeling and neuronal health, PLA2G6 influences diverse cellular processes such as cell signaling, oxidative stress responses, and inflammation. Its activity contributes to the liberation of lipid second messengers that can modulate the cell cycle, regulate apoptotic processes, and even control innate immune cell migration and superoxide production. Detailed biochemical and structural studies have revealed that the enzyme’s activity is finely tuned by protein interactions and intracellular signaling molecules, while its dysregulation may promote ferroptotic cell death and affect tumor biology as well as pancreatic β‑cell function. Together, these findings position PLA2G6 as a central regulator of lipid homeostasis and signal transduction with far‐reaching impacts on cellular physiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christopher M Jenkins, David J Mancuso, Wei Yan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M407841200"}], "href": "https://doi.org/10.1074/jbc.M407841200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15364929"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15364929"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Sun Jun Kim, Debra Gershov, Xiaojing Ma, et al. 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