Phosphorylation of Rho GDI stabilizes the Rho A-Rho GDI complex in neutrophil cytosol.
Biochem Biophys Res Commun
; 218(1): 54-60, 1996 Jan 05.
Article
em En
| MEDLINE
| ID: mdl-8573175
ABSTRACT
The GDP dissociation inhibitor Rho GDI from bovine neutrophil cytosol was purified in association with prenylated Rho A. Upon treatment of this complex with alkaline phosphatase, the Rho A and Rho GDI components were released to their free forms. Following migration in 2D-PAGE and specific immunodetection, the shape of the spot of Rho GDI was found to depend markedly on whether Rho GDI subjected to electrophoresis was present in a Rho A-Rho GDI complex or in a free form. In the first case Rho GDI focused as an elongated spot between pI 5.2 and pI 4.6 whereas in the later case it focused at a pI of 5.0-5.2 as a round spot. Activation of neutrophils by anaphylatoxin C5a in a [32Pi] supplemented medium resulted in radiolabeling of Rho GDI. In vitro incubation of Rho GDI with a neutrophil homogenate in the presence of [gamma 32P] ATP led also to radiolabeling of Rho GDI. Taken together these results suggest that Rho GDI in the Rho A-Rho GDI complex is phosphorylated and that the stability of the complex depends on the phosphorylation state of Rho GDI.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Ligação ao GTP
/
Inibidores de Dissociação do Nucleotídeo Guanina
/
Neutrófilos
Limite:
Animals
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article