Elastic network model reveals distinct flexibilities of capping proteins bound to CARMIL and twinfilin-tail.

Autor: Koike R; Graduate School of Informatics, Nagoya University, Nagoya, Japan., Ota M; Graduate School of Informatics, Nagoya University, Nagoya, Japan.; Institute for Glyco-core Research, Nagoya University, Nagoya, Japan.
Jazyk: angličtina
Zdroj: Proteins [Proteins] 2024 Jan; Vol. 92 (1), pp. 37-43. Date of Electronic Publication: 2023 Jul 27.
DOI: 10.1002/prot.26560
Abstrakt: Capping protein (CP) binds to the barbed end of an actin-filament and inhibits its elongation. CARMIL binds CP and dissociates it from the barbed end of the actin-filament. The binding of CARMIL peptide alters the flexibility of CP, which is considered to facilitate the dissociation. Twinfilin also binds to CP through its C-terminal tail. The complex structures of the CP/twinfilin-tail (TW-tail) peptide indicate that the binding sites of CARMIL and TW-tail overlap. However, TW-tail binding does not facilitate the dissociation of CP from the barbed end. We extensively investigated the flexibilities of CP in the CP/TW-tail or CP/CARMIL complexes using an elastic network model and concluded that TW-tail binding does not alter the flexibility of CP. Our extensive analysis also highlighted that the strong contacts of peptides with the two domains of CP, that is, the CP-L and CP-S domains, are key to changing the flexibilities of CP. CARMIL peptides can interact strongly with both of the domains, while TW-tail peptides exclusively interact with the CP-S domain because the binding site of TW-tail on CP relatively shifts to the CP-S domain compared with that of CP/CARMIL. This result supports our hypothesis that the dissociation of CP from the barbed end is regulated by the flexibility of CP.
(© 2023 Wiley Periodicals LLC.)
Databáze: MEDLINE
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