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• W3132004252 endingPage "166891" @default.
• W3132004252 startingPage "166891" @default.
• W3132004252 abstract "• Twinfilin binds CP via TWtail that has sequence similarity to CARMIL CPI. • Here we present the crystal structure of CP in complex with TWtail. • TWtail and CARMIL CPI restrict CP in distinct conformations. • Unlike CARMIL CPI, TWtail forms a stable ternary complex with CP and V-1. • Our data suggest that TWtail acts cooperatively with V-1 to destabilize F-actin. Twinfilin is a conserved actin regulator that interacts with actin capping protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity with the CP interaction (CPI) motif of CARMIL. Here we report the crystal structure of TWtail in complex with CP. Our structure showed that although TWtail and CARMIL CPI bind CP to an overlapping surface via their middle regions, they exhibit different CP-binding modes at both termini. Consequently, TWtail and CARMIL CPI restrict the CP in distinct conformations of open and closed forms, respectively. Interestingly, V-1, which targets CP away from the TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique CP-binding motif that regulates CP in a manner distinct from CARMIL CPI." @default.
• W3132004252 created "2021-03-01" @default.
• W3132004252 creator A5004774267 @default.
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• W3132004252 date "2021-04-01" @default.
• W3132004252 modified "2023-10-18" @default.
• W3132004252 title "Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail" @default.
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• W3132004252 doi "https://doi.org/10.1016/j.jmb.2021.166891" @default.
• W3132004252 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33639213" @default.
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