{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPGAM1 is a central glycolytic enzyme that catalyzes the reversible conversion of 3‐phosphoglycerate to 2‐phosphoglycerate, thereby governing glycolytic flux and indirectly regulating anabolic pathways such as the pentose phosphate pathway and serine biosynthesis. In rapidly proliferating cells – particularly in cancers – this enzyme’s activity is modulated by substrate‐induced histidine phosphorylation (for example, by phosphoenolpyruvate and 2,3‐bisphosphoglycerate) that can decouple ATP production from phosphotransfer. Such biochemical tuning supports the high glycolytic rate needed for biomass accumulation and tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its metabolic role, PGAM1 exerts non‐metabolic functions that impact cancer cell survival and dissemination. It has been shown to interact with the cytoskeleton—facilitating invadopodia and podosome formation—to promote cell motility and metastasis, and it also contributes to the repair of DNA double–strand breaks through the stabilization of repair factors. PGAM1’s activity is finely regulated by post–translational modifications such as acetylation (mediated by deacetylases like Sirt1), tyrosine phosphorylation (which enhances substrate binding), and even by its dynamic C–terminal conformational changes. Moreover, additional layers of regulation by microRNAs and circular RNAs further adjust PGAM1 expression and function in tumor cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, PGAM1 is frequently overexpressed in a wide spectrum of malignancies—including non–small cell lung cancer, pancreatic ductal adenocarcinoma, urothelial bladder cancer, prostate cancer, breast cancer, glioma, ovarian cancer, and osteosarcoma—with its upregulation correlating with enhanced glycolysis, aggressive tumor behavior, metastasis, and poor patient prognosis. Inhibition or silencing of PGAM1 has been demonstrated to reduce tumor growth, impair invasion and migration, overcome chemoresistance, and even synergize with immunotherapeutic strategies. Conversely, congenital PGAM1 deficiency produces a distinct myopathic syndrome characterized by exercise–induced cramps and myoglobinuria, underscoring its pivotal role in normal energy metabolism. Structural investigations of PGAM1 have further provided insights into its dynamic active site, fueling the rational design of selective inhibitors with potential therapeutic impact."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Matthew G Vander Heiden, Jason W Locasale, Kenneth D Swanson, et al. 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