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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
Author(s) -
Persson Cathrine,
Carballeira Nivia,
WolfWatz Hans,
Fällman Maria
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.9.2307
Subject(s) - biology , focal adhesion , tyrosine , phosphorylation , tyrosine phosphorylation , yersinia , protein tyrosine phosphatase , microbiology and biotechnology , ptk2 , biochemistry , genetics , bacteria , mitogen activated protein kinase kinase , protein kinase a
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.