Biology: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 | ||||||||
| SCOP2 | 1rho / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 91 | ||||||||
| OPM protein | 1qvy | ||||||||
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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
ARHGDIA; ARHGDIB; ARHGDIG;
References
- ↑ "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. May 1997. doi:10.1016/S0969-2126(97)00218-9. PMID 9195882.
- ↑ "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. 1993. doi:10.1111/j.1432-1033.1993.tb18264.x. PMID 8223583.
- ↑ 3.0 3.1 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.
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