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RHO protein GDP dissociation inhibitor

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

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. 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. Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases. The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.

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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