DEP domain
{{Infobox protein family
| Symbol = DEP
| Name = Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP)
| image = PDB 1fsh EBI.jpg
| width =
| caption = structural basis of the recognition of the dishevelled dep domain in the wnt signaling pathway
| Pfam = PF00610
| Pfam_clan =
| InterPro = IPR000591
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD = cd04371
}}
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 in RGS9.{{Cite journal
| last1 = Masuho | first1 = I.
| last2 = Wakasugi-Masuho | first2 = H.
| last3 = Posokhova | first3 = E. N.
| last4 = Patton | first4 = J. R.
| last5 = Martemyanov | first5 = K. A.
| title = Type 5 G Protein Subunit (G 5) Controls the Interaction of Regulator of G Protein Signaling 9 (RGS9) with Membrane Anchors
| doi = 10.1074/jbc.M111.241513
| journal = Journal of Biological Chemistry
| volume = 286
| issue = 24
| pages = 21806–21813
| year = 2011
| doi-access = free
| pmid = 21511947
| pmc =3122235
}}
- 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.{{cite journal | author = Burchett SA | title = Regulators of G protein signaling: a bestiary of modular protein binding domains | journal = J. Neurochem. | volume = 75 | issue = 4 | pages = 1335–51 |date=October 2000 | pmid = 10987813 | doi = 10.1046/j.1471-4159.2000.0751335.x| doi-access = }}{{cite journal |vauthors=Wong HC, Mao J, Nguyen JT, Srinivas S, Zhang W, Liu B, Li L, Wu D, Zheng J | title = Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway | journal = Nat. Struct. Biol. | volume = 7 | issue = 12 | pages = 1178–84 |date=December 2000 | pmid = 11101902 | doi = 10.1038/82047 | pmc = 4381838 }} 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.