Active Rho Detection Kit

The Ras superfamily of small GTP-binding proteins comprise a large class of proteins that can be classified into at least five families based on their sequence and functional similarities: Ras, Rho, Rab, Arf, and Ran. 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 progression, cell survival, actin cytoskeletal organization, cell polarity and movement, and vesicular and nuclear transport. An upstream signal stimulates the dissociation of GDP from the GDP-bound form, which leads to the binding of GTP and formation of the GTP-bound form. The activated G protein then goes through a conformational change in its downstream effector-binding region, leading to the binding and regulation of downstream effectors. This activation can be switched off by the intrinsic GTPase activity, which hydrolyzes GTP to GDP and releases the downstream effectors. These intrinsic guanine nucleotide exchange and GTP hydrolysis activities of Ras superfamily proteins are also regulated by guanine nucleotide exchange factors that promote formation of the active GTP-bound form and GTPase activating proteins that return the GTPase to its GDP-bound inactive form.Rho family small GTPases, including Rho, Rac, and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation, and differentiation. They are activated by guanine nucleotide exchange factors, which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins, which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor. RhoA, RhoB and RhoC are highly homologous, but appear to have divergent biological functions. Carboxy-terminal modifications and differences in subcellular localization allow these three proteins to respond to and act on distinct signaling molecules.

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