{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPhosphoglycerate kinase 1 (PGK1) is a pivotal enzyme in glycolysis that not only catalyzes the reversible transfer of a phosphoryl group to generate ATP but also functions as an atypical protein kinase that integrates metabolic reprogramming with oncogenic signaling. Under conditions such as hypoxia and oncogenic stimulation, PGK1 undergoes mitochondrial translocation where it phosphorylates key targets (for example, pyruvate dehydrogenase kinase 1), thereby suppressing mitochondrial pyruvate utilization and reinforcing the Warburg effect to promote tumor growth. In parallel, post‐translational modifications like acetylation fine‐tune its catalytic efficiency by altering substrate affinity and domain dynamics, underscoring its multifunctional role in cellular energy homeostasis and proliferation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its intracellular metabolic duties, PGK1 is actively secreted by tumor cells where it performs a disulphide reductase activity that converts plasmin into angiostatin, thereby modulating angiogenesis. Its cellular levels and stability are controlled by a network of regulatory mechanisms that include long noncoding RNAs—such as MetaLnc9 and LINC00926—which affect its ubiquitination status, as well as transcriptional and post‐transcriptional regulators including tumor suppressors (e.g. PTEN), nuclear receptors (e.g. PPARγ) and microRNAs (for instance, miR‐450b-3p). These regulatory events culminate in the activation of downstream oncogenic pathways, notably AKT/mTOR and CXCR4-mediated cascades, ultimately promoting tumor invasion, metastasis, and resistance to targeted therapies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDetailed structural and mutational studies have revealed that PGK1 exists predominantly in an open conformation that transiently closes upon substrate binding—a transition critically mediated by key residues such as Lys215 and Arg38. Disruptive mutations in PGK1 not only impair catalytic function but also compromise protein stability, leading to an aggregation‐prone state that underlies a spectrum of PGK1 deficiency disorders marked by hemolytic anemia, neurological dysfunctions, and myopathies. In addition, noncanonical roles for PGK1 have emerged; it participates in DNA replication as a component of primer recognition complexes and is instrumental in the phosphorylation of l-nucleoside analog diphosphates, a step that influences the efficacy of antiviral and anticancer agents."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "22"}, {"type": "fg_f", "ref": "10"}, {"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPGK1’s dysregulation is implicated in a broad range of pathological states extending beyond classical cancer metabolism. In gastric and colon cancers, aberrant PGK1 expression modulates CXCR4 and β-catenin signaling to enhance invasiveness, while in breast, kidney, and oral squamous cell carcinomas, its upregulation is associated with metabolic reprogramming, treatment resistance, and poor clinical outcome. Moreover, altered PGK1 levels correlate with defects in follicular cell competence, influence nucleoside analog metabolism, and even contribute to conditions such as osteoblast oxidative injury, endometrial chemoresistance, and the hormonal disturbances observed in polycystic ovary syndrome. Collectively, these studies underscore the multifaceted nature of PGK1 as both an essential metabolic enzyme and a central node in signaling networks that govern cell survival, proliferation, and adaptive responses to stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xinjian Li, Yuhui Jiang, Jill Meisenhelder, et al. 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