{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nST6GAL1 is a key glycosyltransferase that catalyzes the addition of α2,6‐linked sialic acids to N‐glycans on membrane and secreted glycoproteins, thereby modulating receptor–ligand interactions and downstream signaling. Its glycosylation of critical immune receptors—including those on developing T cells and macrophages—protects against ligand‐induced apoptosis by limiting recognition by galectins and death receptor complex formation. This enzymatic modification has been shown to block galectin‐1–induced thymocyte death, reduce Fas receptor–mediated apoptosis, and modulate TNF receptor internalization, thus promoting cell survival in immune cells and liver tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer, ST6GAL1 is frequently upregulated and contributes to multiple hallmarks of tumor progression. Enhanced α2,6‐sialylation by ST6GAL1 alters cell–cell and cell–matrix adhesion, promotes epithelial–mesenchymal transition (EMT), sustains cancer stem cell features, and confers resistance to apoptosis and chemotherapeutics. In diverse malignancies—including colon, cervical, gastric, prostate, ovarian, lung, pancreatic, osteosarcoma, and hematologic tumors—ST6GAL1‐mediated sialylation affects integrin stabilization, growth factor receptor signaling (e.g., EGFR, Notch1, and FGFR1), and hypoxia‐inducible signals, thereby fostering invasive behavior, metastatic potential, and therapeutic resistance. These studies also underscore its association with altered mRNA isoforms and epigenetic regulation, linking its dysregulation to tumor aggressiveness and poor prognosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its catalytic function in glycan maturation, structural and regulatory studies of ST6GAL1 have revealed additional mechanisms that influence its activity and clinical utility. Proteolytic cleavage by BACE1 releases a soluble form of ST6GAL1 that can modify extracellular glycoproteins and may serve as a systemic regulator of cell adhesion and survival. Structural analyses have elucidated the enzyme’s substrate specificity and catalytic mechanism, while epigenetic and post‐transcriptional controls—including modulation by noncoding RNAs and external stressors such as alcohol exposure—further impact its expression. These insights have paved the way for exploiting ST6GAL1 not only as a biomarker for disease progression in cancers and liver pathologies but also as a potential therapeutic target to overcome drug resistance, as seen with altered receptor sialylation affecting monoclonal antibody efficacy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Maho Amano, Marisa Galvan, Jiale He, et al. 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