Members of the Ras superfamily of small GTP-binding proteins are critical mediators of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization ａnd secretion. The counter-conversion of the active GTP-bound form of these proteins to their inactive GDP-bound form is influenced by two types of regulatory proteins: those that alter the intrinsic GTPase activity of the GTP-binding proteins ａnd those that alter the rate of GDP/GTP exchange. Guanine nucleotide-releasing factors (GRFs) increase the GDP dissociation rate, while GDP-dissociation inhibitors (GDIs) decrease the dissociation rate. Rho GDIα, also known as ARHGDIA or GDIA1, is a 204 amino acid member of the Rho GDI family of proteins. Localized to the cylasm, Rho GDIα inhibits the dissociation of GDP from Rho proteins, thereby preventing GTP from binding to ａnd subsequently activating Rho proteins. In humans, Rho GDIα can be phosphorylated at Ser 101 by p21-activated kinase (αPAK), an event that inhibits Rho GDIα activity ａnd may result in positive feedback regulation of certain Rho GDIα target proteins.
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Recombinant protein

WBICCFC

HumanMouseMonkey