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Gastrin stimulates the formation of a p60 Src /p125 FAK complex upstream of the phosphatidylinositol 3‐kinase signaling pathway
Author(s) -
Daulhac Laurence,
Kowalski-Chauvel Aline,
Pradayrol Lucien,
Vaysse Nicole,
Seva Catherine
Publication year - 1999
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/s0014-5793(99)00129-5
Subject(s) - phosphatidylinositol , signal transduction , kinase , proto oncogene tyrosine protein kinase src , gastrin , chemistry , phosphorylation , microbiology and biotechnology , biology , biochemistry , secretion
The molecular events whereby gastrin occupancy of G/CCK B receptors leads to phosphatidylinositol (PI) 3‐kinase activation have been examined. We report here that this peptide promotes the association between two non‐receptor tyrosine kinases, p60 Src and p125 FAK , and elicits a parallel increase in tyrosine phosphorylation and activity of both kinases. Gastrin‐induced PI 3‐kinase activity was coprecipitated with p60 Src and p125 FAK and was inhibited by herbimycin A, the selective Src inhibitor PP‐2 or cytochalasin D, which disrupts the actin cytoskeleton and prevents p125 FAK activity. These results indicate, for the first time, that a p60 Src /p125 FAK complex acts upstream of the gastrin‐stimulated PI 3‐kinase pathway.