{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein L‐isoaspartyl methyltransferase (PCMT1), also known as PIMT, is a highly conserved carboxyl methyltransferase that plays a critical role in “repairing” damaged proteins. By recognizing and methylating aberrant isoaspartyl and D‐aspartyl residues—common products of spontaneous protein aging and stress—it helps restore the normal L‐aspartyl configuration, thereby maintaining proper protein structure and function. Structural and mechanistic studies have revealed key nucleotide binding domains essential for catalysis, while genetic studies further associate PCMT1 with developmental processes; for example, its altered expression is linked to neural tube defects and premature ovarian failure, and its function is central to cell‐signaling cascades in diverse organisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant expression or altered activity of PCMT1 is increasingly implicated in cancer progression. In multiple tumor types—including bladder, lung, breast, prostate, liver, gastric cancers, and gliomas—PCMT1 is frequently overexpressed and appears to promote aggressive behaviors such as enhanced migration, invasion, and epithelial–mesenchymal transition. For instance, PCMT1‐mediated methylation of specific isoaspartyl residues on tumour suppressor proteins (e.g. p53) can destabilize these proteins and dampen their anti‐tumor activities. Moreover, acting as a transcriptional coactivator (for example, in estrogen receptor–mediated gene activation), PCMT1 further contributes to oncogenic signaling cascades. Taken together, these findings support the view of PCMT1 as an unfavorable prognostic marker and a potential therapeutic target in a wide range of malignancies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond protein repair and tumor biology, PCMT1 has been implicated in a number of other critical cellular processes including neuroprotection and metabolic regulation. In neuronal systems, for example, PCMT1 helps counteract oxidative stress—protecting cells from dopamine‐induced apoptosis and modulating amyloid β oligomer formation, which is pertinent to Alzheimer’s disease pathogenesis. Furthermore, PCMT1 influences hepatic gluconeogenesis and mitochondrial architecture, linking its activity to overall metabolic homeostasis and inflammatory responses observed in conditions such as coronary artery disease and chronic lung disorders. These diverse roles underscore PCMT1 as an integrative regulator at the crossroads of protein quality control, signal transduction, and disease pathogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Carsten Ryttersgaard, Scott C Griffith, Michael R Sawaya, et al. 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