Phosphorylation of p125FAK and paxillin focal adhesion proteins in src‐transformed cells with different metastatic capacity

FEBS Letters

Tatosyan, Alexander¹  Tavitian, Armand²  Schramm, Kira³  Musatkina, Elena¹  Kreuser, Ernst-Dietrich³  Rodina, Anna¹ 

[1]Institute of Carcinogenesis, Cancer Research Center, Kashirskoye shosse 24, 115478 Moscow, Russia

[2]INSERM, U.248, Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France

[3]Universitätsklinikum Benjamin Franklin, Hindenburgdamm 30, Tibor- Diamantstein-Haus, 122200 Berlin, Germany

关键词: V-src;    Metastasis;    Focal adhesion kinase;    Paxillin;    Hamster cell;    Tyrosine phosphorylation;    FAK;    focal adhesion kinase;    Csk;    carboxy-terminus src kinase;    HM;    high metastatic;    LM;    low metastatic;    RSV;    Rous sarcoma virus;    PMSF;    phenylmethylsulfonyl fluoride;    mAbs;    monoclonal antibodies;   

DOI  :  10.1016/S0014-5793(99)00794-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown