{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTissue transglutaminase 2 (TG2) is a highly versatile, calcium‐dependent enzyme that carries out protein cross‐linking via transamidation and deamidation reactions, and—remarkably—also exhibits intrinsic kinase activity. Structural studies have revealed that TG2 can adopt an extended, activated conformation in which its active site is exposed within a tunnel formed by key aromatic residues that separate its acyl–donor and –acceptor substrates. These catalytic reactions not only allow TG2 to form stable, covalently cross‐linked protein networks but also enable it to phosphorylate specific substrates such as insulin‐like growth factor–binding protein–3, p53 and even certain histone residues. In addition, nonenzymatic protein–protein interactions mediated by TG2 further expand its functional repertoire."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its catalytic versatility, TG2 plays a central role in remodeling the extracellular matrix (ECM) and in regulating cell–matrix interactions. By cross‐linking structural proteins and binding tightly to fibronectin, TG2 promotes the assembly and stabilization of ECM networks. This activity enhances focal adhesion formation and integrin signalling, modulating cell adhesion, spreading, and migration, and even influencing epithelial–mesenchymal transition (EMT). Such signalling effects are mediated via direct associations with cell surface receptors—including integrins and syndecans—which in turn activate downstream survival and anti‐apoptotic pathways (for example, via NF‐κB and Akt), thereby contributing to chemoresistance and enhanced invasive behaviour."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "19"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTG2’s dysregulated expression and activity have been implicated in a wide spectrum of pathological settings. In celiac disease, for example, TG2 is both the target of autoantibodies and the enzyme that deamidates gluten peptides—thereby enhancing their binding to HLA‐DQ2/8 molecules and provoking T‐cell–mediated intestinal injury. In other inflammatory and neurodegenerative disorders, as well as in vascular conditions, its modulation by the redox environment (and by factors such as thioredoxin) influences extracellular signalling and tissue remodelling. Notably, in various cancers—including breast, melanoma, pancreatic and ovarian tumors—chronic TG2 expression promotes cell survival, resistance to chemotherapeutic agents, EMT, and metastasis by rewiring intracellular signalling networks and fostering a cancer stem cell phenotype. Moreover, emerging evidence even links aberrant TG2 activity with altered processing of proteins implicated in diseases such as Parkinson’s and Alzheimer’s."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "35"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Burkhard Fleckenstein, Øyvind Molberg, Shuo-Wang Qiao, et al. 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