{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTPM2, which encodes the β‐tropomyosin isoform, is an essential component of the thin filament in striated muscle where it binds along actin filaments and regulates actin–myosin interactions in a Ca²⁺‐dependent fashion. In normal muscle, proper head‐to‐tail polymerization of TPM2 not only helps stabilize the actin filament but also fine‐tunes the formation and cycling of myosin cross-bridges to enable effective force generation. Several studies have demonstrated that specific TPM2 mutations disrupt its affinity for actin, alter Ca²⁺ sensitivity and affect cross-bridge kinetics—phenomena that manifest in a spectrum of congenital myopathies (including nemaline myopathy, cap disease, congenital fibre type disproportion, and distal arthrogryposis) as well as in clinical conditions such as Escobar syndrome. In patients, mutant TPM2 proteins show impaired incorporation into the sarcomere, disturbances in cooperative thin filament activation, and defects in the head-to-tail interactions that normally underlie muscle contraction and stability. These defect(s) thereby lead to either hypercontractile or hypocontractile phenotypes depending on the specific amino acid change and its impact on structural dynamics and actomyosin regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in muscle, TPM2 also contributes importantly to the regulation and stabilization of the actin cytoskeleton in non‐muscle cells. Alterations in TPM2 expression have been linked to changes in cellular rigidity, stress fiber organization, and intracellular transport. For example, TPM2 helps modulate local contractile events for rigidity sensing on the extracellular matrix as well as the initiation and termination of motor protein–driven runs along microtubules. Moreover, aberrant TPM2 expression or splicing is emerging as a potential biomarker in various cancers—including ovarian, prostate, breast, and glioblastoma—as well as in other pathological contexts such as atherosclerosis and neuroendocrine tumors. In these settings, dysregulation of TPM2 is thought to impact cell proliferation, migration, and epithelial–mesenchymal transition by altering cytoskeletal dynamics and cellular adhesion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alain Expert-Bezançon, Alain Sureau, Patrice Durosay, et al. 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