Abstract
The heterodimeric actin-capping protein (CP) is a major capper of barbed ends of actin filaments in eukaryotes, which prevents the incorporation or loss of actin subunits. CP regulates actin-dependent events in cells, including controlling cell shape and movement. CP is regulated by CARMIL, which inhibits CP in vitro and proposed to be able to physically remove CP from actin filaments. Here, we have identified the residues on the surface of CP that are important for binding to actin and to CARMIL. Previous cryo EM studies and computational docking studies predicted the residues involved in the interaction of CP and actin filaments, and functional assays with site-directed mutants of CP confirmed the predictions. Using TIRF (total internal reflection fluorescence) microscopy, we observed that adding CARMIL rapidly changed capped actin filaments to grow, consistent with uncapping. Together, these results extend our understanding of how CP binds to the barbed end of the actin filament.
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