Rho GTPase-activating proteins in cell regulation.

By S. Moon, Yi Zheng. Trends in Cell Biology, 2003

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Rho-family GTPases: it's not only Rac and Rho (and I like it) (2004, background): “…GAPs, which stimulate the intrinsic GTP hydrolysis activity of Rho-family proteins and thereby promote formation of the inactive GDP-bound protein (Moon and Zheng, 2003); and (3) GDIs, which inhibit Rho proteins by blocking nucleotide exchange, and thus the binding of effectors and GAPs to…”
Cell migration: Rho GTPases lead the way. (2004, background): “…proteins (GAPs) negatively regulate the switch by enhancing its intrinsic GTPase activity and guanine nucleotide dissociation inhibitors (GDIs) are thought to block the GTPase cycle by sequestering and solubilizing the GDP-bound form (Moon and Zheng, 2003; Schmidt and Hall, 2002; Zheng, 2001).”
Rac and Rho GTPases in cancer cell motility control (2010, background): “Indeed, external to their GEF or GAP domains, these proteins strongly diverge in structure and secondary functions [6,13].”
The Ras superfamily at a glance (2005, background): “Reflecting their involvement in such a diversity of cellular processes, RhoA, Rac1 and Cdc42 proteins are each regulated by a surprising diversity of GEFs and GAPs (Schmidt and Hall, 2002; Moon and Zheng, 2003 ) and utilize a similarly diverse set of downstream effectors (Bishop and Hall, 2000).”