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Phosphorylation of p125 FAK and paxillin focal adhesion proteins in src‐transformed cells with different metastatic capacity
Author(s) -
Rodina Anna,
Schramm Kira,
Musatkina Elena,
Kreuser Ernst-Dietrich,
Tavitian Armand,
Tatosyan Alexander
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)00794-2
Subject(s) - paxillin , proto oncogene tyrosine protein kinase src , focal adhesion , phosphorylation , tyrosine phosphorylation , microbiology and biotechnology , rous sarcoma virus , ptk2 , tyrosine , biology , signal transduction , cancer research , protein phosphorylation , chemistry , biochemistry , protein kinase a , gene , mitogen activated protein kinase kinase
Hamster fibroblasts transformed by Rous sarcoma virus (RSV) display different metastatic potentials that are associated with specific structural features of the v‐src oncoprotein. This diverse metastatic activity could be due to various tyrosine phosphorylation levels of specific src protein substrates. To check this hypothesis, phosphorylation of the FAK and paxillin proteins, involved in signal transduction pathways and known as src protein substrates, was tested. It was shown that FAK and paxillin are hyperphosphorylated in the high metastatic cell lines as compared with the phosphotyrosine level of these proteins found in the low metastatic cell lines. In addition, our data confirm that v‐src protein plays a direct role in paxillin phosphorylation.