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Smoothelin-like protein 2 is a cytoskeletal regulatory protein highly expressed in skeletal muscle and epithelial tissues, involved in actin filament organization and stabilization of the apical cortex[1][3][4][6]. It contains a calponin homology domain and binds actin directly, modulating turnover in part via inhibition of coronin-1B[1][3][4]. SMTNL2 is a substrate of MAP kinases such as JNK1-3 and ERK2, being phosphorylated at specific sites critical for its function during muscle differentiation and epithelial morphogenesis[2][1]. Expression is developmentally regulated and concentrated at sites of junctional and apical actin in epithelia and during myocyte differentiation[3][4]. There are no validated therapeutic drugs or biomarker applications at present; the molecule is primarily of research interest in cellular cytoskeleton regulation and morphogenesis[1][2][3][4][6].
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