Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 433, Issue 9, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2021.166891
Keywords
twinfilin; actin capping protein; actin dynamics; V-1; conformational flexibility
Categories
Funding
- JSPS KAKENHI [25650064, 16K17708, 20K06522, 17K07373, 18K12217, 19H05390]
- BINDS from AMED [20am0101111j0004]
- Grants-in-Aid for Scientific Research [20K06522, 25650064, 17K07373, 16K17708, 18K12217, 19H05390] Funding Source: KAKEN
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Twinfilin interacts with actin capping protein (CP) in a unique way, regulating CP structure distinct from CARMIL. TWtail and CARMIL CPI restrict CP in different conformations, indicating their unique binding modes with CP.
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. (C) 2021 Elsevier Ltd. All rights reserved.
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