DEP domain

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP)
structural basis of the recognition of the dishevelled dep domain in the wnt signaling pathway
Identifiers
Symbol	DEP
Pfam	PF00610
InterPro	IPR000591
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In molecular biology, the DEP domain (Dishevelled, Egl-10 and Pleckstrin domain) is a globular protein domain of about 80 amino acids that is found in over 50 proteins involved in G-protein signalling pathways. It was named after the three proteins it was initially found in:

• Dishevelled (Dsh and Dvl), which plays a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus; it is a segment polarity protein required to establish coherent arrays of polarised cells and segments in embryos, and plays a role in wingless signalling.

• Egl-10, which regulates G-protein signalling in the central nervous system.

• Pleckstrin, the major substrate of protein kinase C in platelets; Pleckstrin contains two PH domains flanking the DEP domain.

Mammalian regulators of G-protein signalling also contain these domains, and regulate signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving them into their inactive GDP-bound form. 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.^[1][2] Nuclear magnetic resonance spectroscopy has revealed that the DEP domain comprises a three-helix bundle, a beta-hairpin 'arm' composed of two beta-strands and two short beta-strands in the C-terminal region.^[2]

References

1. ^ Burchett SA (October 2000). "Regulators of G protein signaling: a bestiary of modular protein binding domains". J. Neurochem. 75 (4): 1335–51. doi:10.1046/j.1471-4159.2000.0751335.x. PMID 10987813. 
2. ^ ^{a b} Wong HC, Mao J, Nguyen JT, Srinivas S, Zhang W, Liu B, Li L, Wu D, Zheng J (December 2000). "Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway". Nat. Struct. Biol. 7 (12): 1178–84. doi:10.1038/82047. PMID 11101902. 

This article includes text from the public domain Pfam and InterPro IPR000591