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==Function==
==Function==
There is currently very little information about the cellular role of this protein. Interestingly, however, Dock6 has been reported to exhibit dual GEF specificity towards the small G proteins [[Rac1]] and [[Cdc42]].<ref name="Miyamoto_2007">{{cite journal | vauthors = Miyamoto Y, Yamauchi J, Sanbe A, Tanoue A | title = Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth| journal = Exp. Cell Res. | volume = 313 | issue = 4 | pages = 791–804|date=February 2007 | pmid = 17196961 | doi = 10.1016/j.yexcr.2006.11.017| url = }}</ref> 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.
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]].<ref name="Miyamoto_2007">{{cite journal | vauthors = Miyamoto Y, Yamauchi J, Sanbe A, Tanoue A | title = Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth| journal = Exp. Cell Res. | volume = 313 | issue = 4 | pages = 791–804|date=February 2007 | pmid = 17196961 | doi = 10.1016/j.yexcr.2006.11.017| url = }}</ref> 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.
Dock6 was identified as one of a family of proteins which share high sequence similarity with Dock180, the archetypal member of the DOCK family.[2] It has a similar domain arrangement to other DOCK proteins,[3] with a DHR1 domain known in other proteins to bind phospholipids,[4] and a DHR2 domain containing the GEF activity.[5]
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.[6] 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 (December 2002). "Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity". J. Cell Sci. 115 (Pt 24): 4901–13. doi:10.1242/jcs.00219. PMID12432077.
↑Meller N, Merlot S, Guda C (November 2005). "CZH proteins: a new family of Rho-GEFs". J. Cell Sci. 118 (Pt 21): 4937–46. doi:10.1242/jcs.02671. PMID16254241.
↑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.
Kwofie MA, Skowronski J (2008). "Specific recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 guanine nucleotide exchange factors". J. Biol. Chem. 283 (6): 3088–96. doi:10.1074/jbc.M705170200. PMID18056264.
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.
