RHO protein GDP dissociation inhibitor
| RHO protein GDP dissociation inhibitor | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of RHO guanine nucleotide dissociation inhibitor.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Rho_GDI | ||||||||
| Pfam | PF02115 | ||||||||
| InterPro | IPR000406 | ||||||||
| SCOP | 1rho | ||||||||
| SUPERFAMILY | 1rho | ||||||||
| OPM superfamily | 99 | ||||||||
| OPM protein | 1qvy | ||||||||
| |||||||||
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.
Human proteins containing this domain
References
- ↑ 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.
- ↑ 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.
- 1 2 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