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 <PDOC50176>) in the DID or
GBD/FH3 domain [1,2,3]. 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 (see
<PDB:2BAP; D>) [3,4] and the C-terminal part of the domain contains several
basic residues that form a basic region [5,6].
Some proteins known to contain a DAD domain:
Fruit fly protein diaphanous, which plays an important role during
Mammalian diaphanous-related formins (DRF) 1-3, which act as Rho GTPase
effectors during cytoskeletal remodeling.
Baker's yeast proteins BNI1 and BNI1-related protein 1 (BNR1).
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
The profile we developed covers the entire DAD domain.
July 2006 / First entry.
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