D4-GDI Antibody – Rabbit Polyclonal

Members of the Rho (or ARH) protein family (see MIM 165390) and other Ras-related small GTP-binding proteins (see MIM 179520) are involved in diverse cellular events, including cell signaling, proliferation, cytoskeletal organization, and secretion. The GTP-binding proteins are active only in the GTP-bound state. At least 3 classes of proteins tightly regulate cycling between the GTP-bound and GDP-bound states: GTPase-activating proteins (GAPs), guanine nucleotide-releasing factors (GRFs), and GDP-dissociation inhibitors (GDIs). The GDIs, including ARHGDIB, decrease the rate of GDP dissociation from Ras-like GTPases (summary by Scherle et al., 1993 [PubMed 8356058]).[supplied by OMIM, Dec 2010]

RhoGDI beta: regulates the GDP/GTP exchange reaction of Rho proteins by inhibiting the dissociation of GDP from them, keeping these small GTPases in an inactive state. The GDIs are made up of two domains: a flexible N-terminal domain of about 70 amino acid residues and a folded 134-residue C-terminal domain. Regulates the GTP/GDP cycling of glucose-responsive small GTPases. Its phosphorylation on Y156, S101, and S174 mediates the cycling of Cdc42 and Rac1 to regulate second-phase insulin secretion. Interacts with WNK1.

Protein type: G protein regulator, misc.; Motility/polarity/chemotaxis; Cell adhesion

Chromosomal Location of Human Ortholog: 12p12.3

Cellular Component: cytoskeleton; cytoplasm; cytoplasmic membrane-bound vesicle; cytosol

Molecular Function: Rho GDP-dissociation inhibitor activity; GTPase activator activity

Biological Process: regulation of small GTPase mediated signal transduction; regulation of catalytic activity; multicellular organismal development; small GTPase mediated signal transduction; immune response; negative regulation of cell adhesion; cell motility; actin cytoskeleton organization and biogenesis; Rho protein signal transduction; positive regulation of GTPase activity