Phosphorylation of Rho GDI stabilizes the Rho A-Rho GDI complex in neutrophil cytosol

被引：27

作者：

Bourmeyster, N ^{[1
]}

Vignais, PV ^{[1
]}

机构：

[1] CEA,DEPT BIOL MOLEC & STRUCT,BCH,LAB BIOCHIM,CNRS,URA 1130,F-38054 GRENOBLE 9,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 218卷 / 01期

关键词：

D O I：

10.1006/bbrc.1996.0011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 [(32)Pi] supplemented medium resulted in radiolabeling of Rho GDI. In vitro incubation of Rho GDI with a neutrophil homogenate in the presence of [gamma(3)P] 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. (C) 1996 Academic Press, Inc.

引用

页码：54 / 60

页数：7

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