Diaphanous Related Formins Are Rho GTPase Effectors That Undergo Autoinhibition

The best-studied subfamily within the formin family of actin nucleators is the diaphanous-related formins (DRFs). In addition to the conserved FH1 and FH2

domains, DRFs contain a GTPase-binding domain (GBD) responsible for the interaction of these proteins with members of the Rho GTPases (Watanabe et al. 1997). Binding of Rho GTPases to the GBD is thought to activate DRFs through relief of autoinhibitory interactions involving additional domains (see below). The majority of our understanding of DRF autoregulation comes from studies of the mammalian homologue of diaphanous (mDia) DRF subgroup, of which there are three isoforms (mDia 1-3). mDia isoforms display overlapping functions in a number of cases (Tominaga et al. 2000; Copeland and Treisman 2002; Peng et al. 2003), and the domains responsible for mDia autoregulation are highly conserved among mDial, mDia2, and mDia3 (Watanabe et al. 1997; Petersen et al. 1998; Alberts 2001). Therefore, for the purpose of clarity the following sections will focus on the best-characterized member of this group, mDia1.

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