{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPSAT1 is a key enzyme of the phosphorylated serine biosynthesis pathway that converts 3‐phosphoglycerate into L‐serine and is expressed in multiple isoforms. Early studies characterized two alternatively spliced human PSAT1 transcripts and demonstrated that the enzyme efficiently catalyzes the reversible conversion of 3‐phosphohydroxypyruvate and L‐glutamate into O‑phospho‑L‑serine, thereby driving serine production even against an energetically unfavorable upstream reaction. Structural analyses have further detailed its three‐dimensional organization, active site architecture and kinetic properties, providing the molecular basis for its function in central nervous system metabolism and hinting at its involvement in neuropsychiatric conditions."}, {"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 metabolic role, germline and somatic defects in PSAT1 have been linked to a spectrum of serine deficiency disorders. In the most severe presentations—such as Neu‐Laxova syndrome—mutations in PSAT1 lead to multisystem developmental anomalies and early lethality, whereas milder variants have been associated with isolated polyneuropathy and skin manifestations. These observations underscore the critical importance of tightly regulated PSAT1 activity during development and neural function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn numerous cancers PSAT1 is overexpressed and its heightened expression correlates with poor prognosis and aggressive tumor behavior. For example, studies in colorectal cancer, esophageal carcinomas, breast tumors (including ER‑negative and triple‐negative subtypes), non‑small cell lung cancer, and cervical and renal cancers demonstrate that PSAT1 upregulation supports tumor cell proliferation, influences cell cycle progression through modulation of factors such as E2F activity and cyclin D1 stability, and contributes to chemoresistance. Moreover, altered PSAT1 levels have been implicated in metabolic reprogramming and serine auxotrophy, while its expression is found to be modulated in part by non‑coding RNA circuits and is associated with features such as immune infiltration, exosomal transfer, and tamoxifen resistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMechanistic studies have revealed multifaceted regulation of PSAT1 that extends beyond its catalytic activity. Post‐transcriptional mechanisms involving microRNA‑145–5p and its sponging by circular RNAs have been shown to modulate PSAT1 levels in colon and ovarian cancers, while a specific p53 codon 72 variant interacts with PSAT1 to influence mitochondrial oxidative phosphorylation and metastatic potential. In addition, modifications such as acetylation and ubiquitination dynamically control PSAT1 stability and turnover. Finally, in KRAS‑driven lung adenocarcinomas, PSAT1 upregulation is coupled with glutamine dependency, and exposure to cigarette smoke further induces PSAT1 to promote protective autophagy in bronchial epithelium, highlighting potential avenues for therapeutic intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joo Youn Baek, Do Youn Jun, Dennis Taub, et al. 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