{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRPM7 is a unique bifunctional protein that combines a Ca²⁺/Mg²⁺‐permeable, nonselective cation channel with an intrinsic serine/threonine kinase domain. Its channel activity displays distinctive properties—including marked outward rectification and strong inhibition by intracellular Mg²⁺ and Mg•nucleotides—and is subject to regulation by various physiological ligands and mechanical forces. Furthermore, TRPM7 can form both homomeric channels and heteromeric complexes (for example, with TRPM6), thereby modulating divalent cation uptake and maintaining cellular magnesium homeostasis. These fundamental properties have been characterized electrophysiologically and biochemically in diverse cell types, establishing TRPM7 as critical for cell viability and ion homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core role in ion transport, TRPM7 critically influences cytoskeletal dynamics and cell adhesion. Activation of its channel function—often in response to mechanical stimuli such as shear stress, membrane stretch, or osmotic swelling—triggers downstream signaling pathways including those mediated by G-proteins, PKA, p38 MAPK, and JNK. These cascades affect actomyosin contractility by, for instance, modulating myosin light chain phosphorylation or calpain activation, thereby altering cell adhesion, migration, and morphogenesis. Such mechanotransduction and cytoskeletal regulatory roles have important implications for cancer cell invasion and metastasis as well as for the modulation of cell–matrix interactions in various tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various pathophysiological contexts, dysregulation of TRPM7 has been linked to disease progression. Altered TRPM7 activity contributes to cancer progression in breast, prostate, and pancreatic tumors by promoting cell proliferation, migration, and metastasis, as well as modifying intracellular signaling (including Notch, STAT3, and AKT pathways) and gene expression through its kinase activity. Its regulatory influence extends to developmental processes, vascular smooth muscle function, immune cell viability, and even bone repair, where TRPM7-mediated cation fluxes and downstream signaling help govern cell survival under stress conditions. Moreover, TRPM7’s role in transducing oxidative and nitrosative stress signals and in modulating zinc compartmentalization further underscores its potential as a therapeutic target in diverse human diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Lillia V Ryazanova, Maxim V Dorovkov, Athar Ansari, et al. 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