Rho GDIα Anticuerpo(C-2): sc-374579

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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 GDIå, also known as ARHGDIA or GDIA1, is a 204 amino acid member of the Rho GDI family of proteins. Localized to the cytoplasm, Rho GDIå inhibits the dissociation of GDP from Rho proteins, thereby preventing GTP from binding to and subsequently activating Rho proteins. In humans, Rho GDIå can be phosphorylated at Ser 101 by p21-activated kinase (åPAK), an event that inhibits Rho GDIå activity and may result in positive feedback regulation of certain Rho GDIå target proteins.