Dock6 (Dedicator of cytokinesis 6), also known as Zir1 is a large (~200 kDa) protein involved in intracellularsignalling networks.[5] It is a member of the DOCK-C subfamily of the DOCK family of guanine nucleotide exchange factors which function as activators of small G proteins.
Dock6 was identified as one of a family of proteins which share high sequence similarity with Dock180, the archetypal member of the DOCK family.[6] It has a similar domain arrangement to other DOCK proteins,[7] with a DHR1 domain known in other proteins to bind phospholipids,[8] and a DHR2 domain containing the GEF activity.[9]
Function[]
There is currently very little information about the cellular role of this protein. However, Dock6 has been reported to exhibit dual GEF specificity towards the small G proteins Rac1 and Cdc42.[10] It is the only DOCK family member reported to activate both of these G proteins. The same study also showed that transfection of the Dock6 DHR2 domain into N1E-115 neuroblastoma cells promoted Rac- and Cdc42-dependent neurite outgrowth, although the physiological significance of this has yet to be demonstrated.
^Côté JF, Vuori K (2006). "In vitro guanine nucleotide exchange activity of DHR-2/DOCKER/CZH2 domains". Meth. Enzymol. Methods in Enzymology. 406: 41–57. doi:10.1016/S0076-6879(06)06004-6. ISBN9780121828110. PMID16472648.
^Miyamoto Y, Yamauchi J, Sanbe A, Tanoue A (February 2007). "Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth". Exp. Cell Res. 313 (4): 791–804. doi:10.1016/j.yexcr.2006.11.017. PMID17196961.
Katoh H, Negishi M (2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 (6947): 461–64. doi:10.1038/nature01817. PMID12879077. S2CID4411133.
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