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• W2059746552 abstract "Diaphanous-related formins (DRFs) regulate the nucleation and polymerization of unbranched actin filaments. The activity of DRFs is inhibited by an intramolecular interaction between their N-terminal regulatory region and a conserved C-terminal segment termed the Diaphanous autoinhibitory domain (DAD). Binding of GTP bound Rho to the mDia1 N terminus releases this autoinhibitory restraint. Here, we describe the crystal structure of the DAD segment of mDia1 in complex with the relevant N-terminal fragment, termed the DID domain. The structure reveals that the DAD segment forms an amphipathic helix that binds a conserved, concave surface on the DID domain. Comparison with the structure of the mDia1 N terminus bound to RhoC suggests that release of the autoinhibitory DAD interaction is accomplished largely by Rho-induced restructuring of the adjacent GTPase binding subdomain (GBD), but also by electrostatic repulsion and a small, direct steric occlusion of the DAD binding cleft by Rho itself." @default.
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• W2059746552 creator A5056841661 @default.
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• W2059746552 date "2006-02-01" @default.
• W2059746552 modified "2023-10-06" @default.
• W2059746552 title "Structure of the Autoinhibitory Switch in Formin mDia1" @default.
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• W2059746552 doi "https://doi.org/10.1016/j.str.2005.12.003" @default.
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