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

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ARHGDIA; ARHGDIB; ARHGDIG;

References

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  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 9195882.623-33&rft.date=1997-05&rft_id=info:doi/10.1016/S0969-2126(97)00218-9&rft_id=info:pmid/9195882&rft.aulast=Keep&rft.aufirst=NH&rft.au=Barnes, M&rft.au=Barsukov, I&rft_id=https://doi.org/10.1016%2FS0969-2126%2897%2900218-9&rfr_id=info:sid/en.wikipedia.org:RHO protein GDP dissociation inhibitor" class="Z3988">
  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 8223583.441-455&rft.date=1993&rft_id=info:doi/10.1111/j.1432-1033.1993.tb18264.x&rft_id=info:pmid/8223583&rft.aulast=Pick&rft.aufirst=E&rft.au=Gorzalczany, Y&rft.au=Engel, S&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1993.tb18264.x&rfr_id=info:sid/en.wikipedia.org:RHO protein GDP dissociation inhibitor" class="Z3988">
  3. ^ a b 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 8796870.129-135&rft.date=1996&rft_id=info:doi/10.1016/1357-4310(96)88723-5&rft_id=info:pmid/8796870&rft.au=Segal AW&rfr_id=info:sid/en.wikipedia.org:RHO protein GDP dissociation inhibitor" class="Z3988">
This article incorporates text from the public domain Pfam and InterPro: IPR000406