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Rho GTPase activity

Moon, S. Y., and Zheng, Y. (2003). Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 13, 13-22. [Pg.225]

Guanine nucleotide exchange factor binds to ras and Grb2 Guanine nucleotide exchange factor binds to Rho GTPase-activating protein binds to Rho... [Pg.68]

DerMardirossian, C., and Bokoch, G.M. (2005). GDIs central regnlatory molecnles in Rho GTPase activation. Trends Cell Biol 15 356-363. [Pg.68]

A. Jain, S.M. Brady-Kalnay, R.V. Bellamkonda, Modulation of Rho GTPase activity alleviates chondroitin sulfate proteoglycan-dependent inhibition of neurite extension, J. Neurosci. Res. 77 (2) (2004) 299-307. [Pg.384]

Saeki, N., Tokuo, H., and Ikebe, M. (2005). BIGl is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity. J. Biol. Chem. 280, 10128-10134. [Pg.183]

Benard, V., and Bokoch, G. M. (2002). Assay of Cdc42, Rac, and Rho GTPase activation by affinity methods. Methods Enzymol. 345, 349-359. [Pg.376]

A subfamily of Rho proteins, the Rnd family of small GTPases, are always GTP-bound and seem to be regulated by expression and localization rather than by nucleotide exchange and hydrolysis. Many Rho GTPase effectors have been identified, including protein and lipid kinases, phospholipase D and numerous adaptor proteins. One of the best characterized effector of RhoA is Rho kinase, which phosphorylates and inactivates myosin phosphatase thereby RhoA causes activation of actomyosin complexes. Rho proteins are preferred targets of bacterial protein toxins ( bacterial toxins). [Pg.1141]

RhoGAP GTPase-activator protein for Rho-like GTPases E(MFP)B 11(11) 21(21) 1AM4... [Pg.204]

Suzuki, N., Nakamura, S., Mano, H., and Kozasa, T. (2003). Gal2 activates Rho GTPase through tyrosine-phosphorylated leukemia-associated RhoGEF. Proc. Natl. Acad. Sri. USA 100, 733-738. [Pg.63]

Subsequent studies have identified Rndl (Oinuma et al, 2003), another member of the Rho GTPase subfamily, and the ErbB-2 tyrosine kinase (Swiercz et al, 2004) in the regulation of RhoA by plexins. Additionally, an apparent requirement for interaction of plexin B with RhoGEFs for potentiation of angiogenesis by semaphorins (Basile et al., 2004) and activation of MAPK pathways (Aurandt et al, 2006) by plexin Bl was identified. Yet, direct evidence for the mechanism by which plexins achieve this activation of RhoA has been elusive. A simple mechanism would be localization of the RhoGEF to membranes on stimulation of the pathway as discussed in Section III.B. Evidence for this comes from a study (Oinuma et al, 2003) with Rndl, which can bind directly to plexin Bl. [Pg.210]


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See also in sourсe #XX -- [ Pg.62 , Pg.159 ]




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