{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPFKP, the platelet‐specific isoform of phosphofructokinase‐1, catalyzes the key rate‐limiting step of glycolysis—namely, the conversion of fructose‑6‑phosphate into fructose‑1,6‑bisphosphate—and thereby serves as a central modulator of cellular energy metabolism. In multiple studies, increased PFKP expression and activity have been shown to drive aerobic glycolysis (“the Warburg effect”), which is critical for promoting rapid cell proliferation and survival. Transcriptional activators such as KLF4 and TARDBP, as well as post‑translational modifications (for example, AKT‐mediated phosphorylation at S386 and EGFR‐driven modifications), have been reported to enhance PFKP stability and enzyme activity, underscoring its pivotal role in metabolic reprogramming in cancer cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical metabolic role, PFKP functions as a versatile regulator that integrates cellular signaling and metabolic flux. In glioblastoma and other malignancies, for instance, PFKP undergoes further regulatory modifications—such as phosphorylation events that drive its plasma membrane or even nuclear translocation—which facilitate downstream activation of pathways including PI3K/AKT, promote VEGF and PD‑L1 expression, and modulate the balance between glycolysis and the pentose phosphate pathway. Moreover, under conditions of cellular stress like nutrient deprivation, PFKP has been reported to act as a protein kinase itself, phosphorylating targets (e.g. ATG4B) to affect autophagy, epithelial–mesenchymal transition, and ultimately metastatic behavior."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, aberrant PFKP expression and genetic variants are correlated with poor patient outcomes and disease progression across a wide spectrum of conditions—from various cancers (including breast, lung, prostate, glioblastoma, melanoma, head and neck, and clear cell renal carcinoma) to metabolic disorders and diabetic complications. Detailed kinetic and promoter studies have not only revealed isoform‑specific properties of PFKP but also implicated its dysregulation—via both genetic polymorphisms and altered post‑translational modifications—in metabolic reprogramming, tumor invasiveness, and even fibrotic processes. Collectively, these findings position PFKP as both a critical driver of oncogenic metabolism and a promising therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jong-Seok Moon, Hee Eun Kim, Eunjin Koh, et al. 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