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Twinfilin-1 (TWF1) is a highly conserved actin-binding protein that regulates the dynamic turnover of actin filaments in eukaryotic cells. It is defined by two ADF/cofilin-like (ADF-H) domains, which allow it to both cap actin filament barbed ends—impeding filament elongation—and sequester actin monomers, preventing their polymerization[2][3][4]. At low pH, twinfilin-1 can sever actin filaments[1][4], and it preferentially caps ADP-bound actin barbed ends[2][4]. TWF1 also interacts with actin capping protein (CP), influencing actin filament dynamics in processes such as cell motility and synaptic function[2][5]. Its two actin-binding domains serve distinct structural and functional purposes in actin interaction and capping[4]. Twinfilin-1 is ubiquitously expressed in mammalian tissues and is essential for normal cellular architecture and function but is not directly established as a therapeutic target or clinical biomarker in current literature.
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