| Autor: |
Rankin, Sara, Morii, Narito, Narumiya, Shuh, Rozengurt, Enrique |
| Zdroj: |
FEBS Letters; January 1994, Vol. 354 Issue: 3 p315-319, 5p |
| Abstrakt: |
In this study we examined the role of rhop21 in neuropeptide-stimulated tyrosine phosphorylation. Intact Swiss 3T3 cells were treated with the Clostridium botulinumC3 exoenzyme which specifically ADP ribosylates and inactivates rhop21. 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 rhop21 is a component of the signal transduction pathway linking seven transmembrane domain receptors with tyrosine phosphorylation and cytoskeletal events. |
| Databáze: |
Supplemental Index |
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