RHO protein GDP dissociation inhibitor
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| RHO protein GDP dissociation inhibitor | |||||||||
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 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.
