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  • Title: Role of bound GDP in the stability of the rho A-rho GDI complex purified from neutrophil cytosol.
    Author: Bourmeyster N, Boquet P, Vignais PV.
    Journal: Biochem Biophys Res Commun; 1994 Nov 30; 205(1):174-9. PubMed ID: 7999019.
    Abstract:
    The rho A-rho GDI complex purified from bovine neutrophil cytosol was found to contain GDP as the only bound nucleotide at a ratio of 1 mol of GDP per mol of complex. The rho GDI component of the complex (pI 4.8-5.0, apparent molecular mass 28-29 kDa) and the rho A component (pI scattered between 5.0-6.2, apparent molecular mass 24 kDa) were resolved by 2D gel electrophoresis. Upon dephosphorylation of bound GDP by apyrase, the rho A component of the complex was prone to proteolytic cleavage. The integrity of rho A in the presence of apyrase was preserved by addition of excess GTP. These data suggest that rho A liganded by GDP in the rho A-rho GDI complex is maintained in a conformation that escapes action of proteases.
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