RHO protein GDP dissociation inhibitor

RHO protein GDP dissociation inhibitor of Rho proteins (rho GDI) regulates GDP/GTP exchange. The protein plays an important role in the activation of the oxygen superoxide-generating NADPH oxidase of phagocytes. This process requires the interaction of membrane-associated cytochrome b559 with 3 cytosolic components: p47-phox, p67-phox and a heterodimer of the small G-protein p21Rac1 and rho GDI.[2] The association of p21rac and GDI inhibits dissociation of GDP from p21rac, thereby maintaining it in an inactive form. The proteins are attached via a lipid tail on p21rac that binds to the hydrophobic region of GDI.[3] Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases.[3] The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.

RHO protein GDP dissociation inhibitor
Structure of RHO guanine nucleotide dissociation inhibitor.[1]
Identifiers
SymbolRho_GDI
PfamPF02115
InterProIPR000406
SCOP21rho / SCOPe / SUPFAM
OPM superfamily91
OPM protein1qvy
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Human proteins containing this domain

ARHGDIA; ARHGDIB; ARHGDIG;

References
  1. Keep NH, Barnes M, Barsukov I, et al. (May 1997). "A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm". Structure. 5 (5): 623–33. doi:10.1016/S0969-2126(97)00218-9. PMID 9195882.
  2. Pick E, Gorzalczany Y, Engel S (1993). "Role of the rac1 p21-GDP-dissociation inhibitor for rho heterodimer in the activation of the superoxide-forming NADPH oxidase of macrophages". Eur. J. Biochem. 217 (1): 441–455. doi:10.1111/j.1432-1033.1993.tb18264.x. PMID 8223583.
  3. Segal AW (1996). "The NADPH oxidase and chronic granulomatous disease". Mol. Med. Today (Regul. Ed.). 2 (3): 129–135. doi:10.1016/1357-4310(96)88723-5. PMID 8796870.
This article incorporates text from the public domain Pfam and InterPro: IPR000406


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