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PROSITE documentation PDOC50186 [for PROSITE entry PS50186]

DEP domain profile





Description

The DEP domain is a globular domain of about 80 residues that is found in more than 50 proteins involved in G protein signaling pathways. It has been named after the three proteins (Dishevelled, Egl-10, and Pleckstrin) in which it was initially identified [1]. It has been proposed that the DEP domain could play a selective role in targeting DEP domain-containing proteins to specific subcellular membranous sites, perhaps even to specific G protein-coupled signaling pathways [2,3].

Nuclear magnetic resonance spectroscopy has revealed that the DEP domain comprises a three-helix bundle, a β-hairpin 'arm' composed of two β-strands and two short β-strands in the C-terminal region [3].

Representative example of proteins containing DEP domains are listed below:

  • Drosophila and vertebrate dishevelled (Dsh and Dvl), proteins that play a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus.
  • Vertebrate Pleckstrin, the major substrate of protein kinase C in platelets. Pleckstrin contains two PH domains (see <PDOC50003>) flanking the DEP domain.
  • Mammalian regulator of G-protein signaling (RGS) proteins 6, 7, 9 and 11 (see <PDOC50132>).
  • Caenorhabditis elegans egl-10, which regulates G protein signaling in nervous system.

The profile we developed covers the entire DEP domain.

Last update:

December 2001 / First entry.

Technical section

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

DEP, PS50186; DEP domain profile  (MATRIX)


References

1AuthorsPonting C.P. Bork P.
TitlePleckstrin's repeat performance: a novel domain in G-protein signaling?
SourceTrends Biochem. Sci. 21:245-246(1996).
PubMed ID8755244

2AuthorsBurchett S.A.
TitleRegulators of G protein signaling: a bestiary of modular protein binding domains.
SourceJ. Neurochem. 75:1335-1351(2000).
PubMed ID10987813

3AuthorsWong H.C. Mao J. Nguyen J.T. Srinivas S. Zhang W. Liu B. Li L. Wu D. Zheng J.
TitleStructural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway.
SourceNat. Struct. Biol. 7:1178-1184(2000).
PubMed ID11101902
DOI10.1038/82047



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