Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin

FEBS Letters

Morii, Narito²  Rozengurt, Enrique¹  Narumiya, Shuh²  Rankin, Sara¹ 

[1] Imperial Cancer Research Fund, PO Box 123, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK;Department of Pharmacology, Kyoto University Faculty of Medicine, Sakyo-ku, Kyoto 606, Japan

关键词: Neuropeptide;    rho p21;    Tyrosine phosphorylation;    FAK;    focal adhesion kinase;    TRITC;    tetramethylrhodamine B isothiocyanate;    FITC;    fluorescein isothiocyanate;    Tyr(P);    tyrosine phosphate;    DMEM;    Dulbecco's modification of Eagle's essential medium;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate buffered saline;    MARCKS;    myristylated alanine-rich protein kinase C substrate;    GRP;    gastrin releasing peptide;    PKC;    protein kinase C;    LPA;    lysophosphatidic acid;   

DOI  :  10.1016/0014-5793(94)01148-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown