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Transgelin (TAGLN) is an actin-binding protein of the calponin family that plays a central role in the regulation and stabilization of the cytoskeleton, particularly in smooth muscle cells and fibroblasts[2][4][5][6]. It is a 22 kDa protein characterized by a calponin homology domain, actin-binding site, and a CLIK motif, and mediates actin cross-linking and cellular contractility[2][5]. TAGLN is involved in differentiation of smooth muscle and other cell types, participates in cell motility and shape change, and serves as an early marker of smooth muscle formation in development and tissue remodeling[2][3][4]. Functionally, it acts as a tumor suppressor and is downregulated in various cancers, making it relevant to cancer progression and a potential biomarker[3][4][7]. TAGLN has also been implicated in the regulation of osteoblast and adipocyte differentiation, in part through its response to TGF-β signaling in mesenchymal stem cells, linking it to regenerative medicine applications[3].
Actin cross-linking and stabilization (modulates cytoskeletal structure and cell contractility); Regulation of TGF-β-induced cell differentiation pathways
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