DAAM1 is a diaphanous-related formin first studied as a novel Dishevelled binding protein and shown to be crucial for the planar cell polarity pathway in Xenopus. DAAM1, like other formins, directs nucleation and elongation of new actin filaments using its conserved formin-homology-2 (FH2) domain. It is a Rho-regulated formin implicated in neuronal development and regulation of gastrulation. It was identified as a binding protein of the Wnt receptor-associated protein Dishevelled. It also binds the GTP-bound RhoA and increases its GTP-bound form population in cells. It exists in an autoinhibited state via intramolecular interactions between its amino-terminal GBD and carboxyl-terminal DAD domains. Structurally the protein includes a GTPase-binding domain (GBD), a diaphanous inhibitory domain (DID), and a coiled-coil region followed by the FH1, FH2 and C-terminal diaphanous auto-regulatory domain (DAD). In humans, the DAAM1 gene is mapped to chromosome 14q23.1.
Disheveled-associated activator of morphogenesis 1; dishevelled-associated activator of morphogenesis 1