Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain

摘要: Abstract Mammalian and fungalDiaphanous-related formin homology (DRF) proteins contain several regions of conserved sequence homology. These include an amino-terminal GTPasebinding domain (GBD) that interacts with activated Rho family members domains mediate targeting or interactions signaling kinases actin-binding proteins. DRFs also a conservedDia-autoregulatory (DAD) in their carboxyl termini binds the GBD. The GBD is bifunctional autoinhibitory regulated by Rho. Expression isolated DAD cells causes actin fiber formation stimulates serum response factor-regulated gene expression. Inhibitor experiments show effects exogenous expression are dependent upon cellular Dia Alanine substitution consensus residues disrupt binding eliminate biological activity. Thus, activates nuclear remodeling mimicking unlatching autoinhibited state complement