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