Diaphanous autoregulatory domain
IPR014767
Definition
Formins participate in the assembly of the actin and microtubule cytoskeletons in processes like cell division, migration, and development. Diaphanous-related formins (DRF) contain an N-terminal GTPase-binding domain (GBD) and a C-terminal diaphanous autoregulatory domain (DAD). DRFs are regulated by an autoinhibitory interaction of the C-terminal DAD with the DRF N-terminal armadillo repeat-like region (see [interpro:IPR000225]) in the DID or GBD/FH3 domain [[cite:PMID:15950879], [cite:PMID:15740615], [cite:PMID:16292343]]. This autoinhibition is released upon competitive binding of an activated Rho GTPase to the GBD. The release of DAD allows the catalytical formin homology 2 (FH2) domain to then nucleate and elongate nonbranched actin filaments. The DAD domain is a ~32 amino acid autoinhibitory domain, which facilitates intramolecular binding. The DAD core forms an α-helical structure and the C-terminal part of the domain contains several basic residues that form a basic region [[cite:PMID:16292343], [cite:PMID:16472745], [cite:PMID:11035012], [cite:PMID:16361707]]. Proteins known to contain a DAD domain include: Fruit fly protein diaphanous, which plays an important role during cytokinesis. Mammalian diaphanous-related formins (DRF) 1-3, which act as Rho GTPase effectors during cytoskeletal remodelling. Saccharomyces cerevisiae (Baker's yeast) proteins BNI1 and BNI1-related protein 1 (BNR1). Emericella nidulans (Aspergillus nidulans) cytokinesis protein sepA, which participates in two actin-mediated processes, septum formation and polarized growth. Mammalian disheveled-associated activator of morphogenesis (DAAM) proteins. Mammalian formin-like 1 protein (Fmnl1) or formin-related protein gene in leukocytes (FRL).
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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