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Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125 FAK and paxillin induced by bombesin and endothelin
Author(s) -
Rankin Sara,
Morii Narito,
Narumiya Shuh,
Rozengurt Enrique
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01148-6
Subject(s) - paxillin , tyrosine phosphorylation , phosphorylation , exoenzyme , microbiology and biotechnology , tyrosine , focal adhesion , ptk2 , bombesin , biology , signal transduction , transmembrane protein , tyrosine kinase , phospholipase c , chemistry , protein kinase c , biochemistry , receptor , neuropeptide , mitogen activated protein kinase kinase , enzyme
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.