Gastrin stimulates the formation of a p60Src/p125FAK complex upstream of the phosphatidylinositol 3-kinase signaling pathway

被引：35

作者：

Daulhac, L ^{[1
]}

Kowalski-Chauvel, A ^{[1
]}

Pradayrol, L ^{[1
]}

Vaysse, N ^{[1
]}

Seva, C ^{[1
]}

机构：

[1] CHU Rangueil, Inst Louis Bugnard, Grp Rech Biol & Pathol Digest, INSERM,U151, F-31403 Toulouse, France

来源：

FEBS LETTERS | 1999年 / 445卷 / 2-3期

关键词：

gastrin; G protein-coupled receptor; phosphatidylinositol; 3-kinase; Src-family kinases; focal adhesion kinase; cellular proliferation;

D O I：

10.1016/S0014-5793(99)00129-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The molecular events whereby gastrin occupancy of G/CCKB 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, (C) 1999 Federation of European Biochemical Societies.

引用

页码：251 / 255

页数：5

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