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The Ras superfamily of small GTP-binding proteins (G proteins) comprise a large class of proteins (over 150 members) that can be classified into at least five families based on their sequence and functional similarities: Ras, Rho, Rab, Arf, and Ran (1,2,3). All these small G proteins have both GDP/GTP-binding and GTPase activities and function as binary switches in diverse cellular and developmental events that include cell cycle preogression, cell survival, actin cytoskeletal organization, cell polarity and movement, and vesicular and nuclear transport (1). An upstream signal stimulates the dissociation of GDP from the GDP-bound form (inactive), which leads to the binding of GTP and entering the GTP-bound form (active). The activated GTP-bound form then goes through conformational change in the its downstream effector-binding region, eventually leads to binding and function regulation of downstream effectors. This activation can be switched off by the intrinsic GTPase activity, which hydrolyzes GTP to GDP and release the downstream effectors. These intrinsic guanine nucleotide exchange and GTP hydrolysis activities of Ras superfamily proteins are also regulated by guanine nucleotide exchange factors (GEFs) that promote formation of the active GTP-bound form and GTPase activating proteins (GAPs) that return the GTPase to its GDP-bound inactive form (4).

1. Takai, Y. et al. (2001) Physiol Rev 81, 153-208.
2. Colicelli, J. (2004) Sci STKE 2004, RE13.
3. Wennerberg, K. et al. (2005) J Cell Sci 118, 843-6.
4. Vigil, D. et al. (2010) Nat Rev Cancer 10, 842-57.

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Zyxin Antibody

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