The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130(Cas) and FAK, and the associated accumulation of these proteins in peripheral focal adhesions

被引：300

作者：

Persson, C ^{[1
]}

Carballeira, N ^{[1
]}

WolfWatz, H ^{[1
]}

Fallman, M ^{[1
]}

机构：

[1] UMEA UNIV, DEPT CELL & MOL BIOL, S-90187 UMEA, SWEDEN

来源：

EMBO JOURNAL | 1997年 / 16卷 / 09期

关键词：

FAK; focal adhesions; p130(Cas); Yersinia; YopH;

D O I：

10.1093/emboj/16.9.2307

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：

Pathogenic Yersinia resist uptake by eukaryotic cells by a mechanism involving the virulence protein YopH, a protein tyrosine phosphatase. We show that p130(Cas) and FAK are phosphorylated and recruited to peripheral focal complexes during bacterial uptake in HeLa cells. The inactive form of YopH interacts with the tyrosine phosphorylated forms of FAK: and p130(Cas) and co-localizes with these proteins in focal adhesions. On the other hand, the presence of active YopH results in inhibition of uptake, dephosphorylation of p130(Cas) and FAK, and disruption of peripheral focal complexes. We suggest that p130(Cas) and FAK are substrates for YopH and that the dephosphorylation of these proteins impairs the uptake of Yersinia pseudotuberculosis into HeLa cells.

引用

页码：2307 / 2318

页数：12

共 65 条

[61]

Vuori K, 1996, MOL CELL BIOL, V16, P2606

[62] TYROSINE PHOSPHORYLATION OF P130(CAS) AND CORTACTIN ACCOMPANIES INTEGRIN-MEDIATED CELL-ADHESION TO EXTRACELLULAR-MATRIX [J].