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Cofilin-2 (CFL2) is a skeletal muscle-specific isoform of the actin-depolymerizing factor (ADF)/cofilin family that is essential for regulating actin filament turnover and sarcomere organization in striated muscle[1][3][5]. It binds both G-actin (monomeric) and F-actin (filamentous) in a 1:1 ratio and modulates actin polymerization and depolymerization in a pH-dependent manner[1][3]. CFL2 plays a critical role in maintaining muscle fiber structure by controlling the length of thin filaments and promoting myoblast differentiation[2][5]. Mutations in CFL2 cause nemaline myopathy type 7, characterized by abnormal actin filament accumulation and muscle weakness[1][2][3][5]. While essential for muscle health, CFL2 is not a direct drug target, and there are currently no therapeutic agents modulating its activity[1][3][5].
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