DEP Domain Containing Protein 4 (DEPDC4)

DEPDC4, Contains 1 DEP domain. The DEP domain shown is from the mDvl1 protein and contains a core helix bundle of three a-helices. H1 and H2 are separated by a ß-hairpin and H3 is followed by two short ß-strands. The triple a-helix architecture forms a hydrophobic core where key residues stabilize the structure through multiple hydrophobic interactions. It has been suggested that the H1 helix is the site of DEP domain interaction with other proteins. Structures to the mouse Epac2 and human Pleckstrin DEP domains share this conserved core structure. DEP domains have been implicated to mediate membrane localization. Furthermore, the DEP domain of a yeast regulator of G-protein signaling, Sst2, has recently been shown to interact with the unphosphorylated C-terminal tail of the yeast GPCR, Ste2, suggesting a role for DEP domains in selective targeting of RGS proteins to specific GPCRs.