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PROSITE documentation PDOC51231 [for PROSITE entry PS51231]

Diaphanous autoregulatory domain (DAD) profile





Description

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 cytokinesis.
  • 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 leukocytes (FRL).

The profile we developed covers the entire DAD domain.

Last update:

July 2006 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

DAD, PS51231; Diaphanous autoregulatory domain (DAD) profile  (MATRIX)


References

1AuthorsHiggs H.N.
TitleFormin proteins: a domain-based approach.
SourceTrends Biochem. Sci. 30:342-353(2005).
PubMed ID15950879
DOI10.1016/j.tibs.2005.04.014

2AuthorsRivero F. Muramoto T. Meyer A.-K. Urushihara H. Uyeda T.Q.P. Kitayama C.
TitleA comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa.
SourceBMC Genomics 6:28-28(2005).
PubMed ID15740615
DOI10.1186/1471-2164-6-28

3AuthorsLammers M. Rose R. Scrima A. Wittinghofer A.
TitleThe regulation of mDia1 by autoinhibition and its release by Rho*GTP.
SourceEMBO J. 24:4176-4187(2005).
PubMed ID16292343
DOI10.1038/sj.emboj.7600879

4AuthorsNezami A.G. Poy F. Eck M.J.
TitleStructure of the autoinhibitory switch in formin mDia1.
SourceStructure 14:257-263(2006).
PubMed ID16472745
DOI10.1016/j.str.2005.12.003

5AuthorsAlberts A.S.
TitleIdentification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain.
SourceJ. Biol. Chem. 276:2824-2830(2001).
PubMed ID11035012
DOI10.1074/jbc.M006205200

6AuthorsWallar B.J. Stropich B.N. Schoenherr J.A. Holman H.A. Kitchen S.M. Alberts A.S.
TitleThe basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain.
SourceJ. Biol. Chem. 281:4300-4307(2006).
PubMed ID16361707
DOI10.1074/jbc.M510277200



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