BOTULINUM C3 EXOENZYME BLOCKS THE TYROSINE PHOSPHORYLATION OF P125(FAK) AND PAXILLIN INDUCED BY BOMBESIN AND ENDOTHELIN

被引：134

作者：

RANKIN, S

MORII, N

NARUMIYA, S

ROZENGURT, E

机构：

[1] IMPERIAL CANC RES FUND,LONDON WC2A 3PX,ENGLAND

[2] KYOTO UNIV,FAC MED,DEPT PHARMACOL,SAKYO KU,KYOTO 606,JAPAN

来源：

FEBS LETTERS | 1994年 / 354卷 / 03期

关键词：

NEUROPEPTIDE; RHO P21; TYROSINE PHOSPHORYLATION;

D O I：

10.1016/0014-5793(94)01148-6

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：

In this study we examined the role of rho p21 in neuropeptide-stimulated tyrosine phosphorylation. Intact Swiss 3T3 cells were treated with the Clostridium botulinum C3 exoenzyme which specifically ADP ribosylates and inactivates rho p21. C3 exoenzyme treatment of cells caused a marked decrease in both bombesin- and endothelin-stimulated tyrosine phosphorylation of multiple proteins, including p125 focal adhesion kinase (FAK) and paxillin. Our results suggest that rho p21 is a component of the signal transduction pathway linking seven transmembrane domain receptors with tyrosine phosphorylation and cytoskeletal events.

引用

页码：315 / 319

页数：5

共 29 条

[11] THE SMALL GTP-BINDING PROTEIN RHO REGULATES THE ASSEMBLY OF FOCAL ADHESIONS AND ACTIN STRESS FIBERS IN RESPONSE TO GROWTH-FACTORS [J].