作者: J.R. Glenney
DOI: 10.1016/S0021-9258(19)47038-5
关键词: Tyrosine phosphorylation 、 Protein phosphorylation 、 Molecular biology 、 SH2 domain 、 Receptor tyrosine kinase 、 Tyrosine kinase 、 Protein tyrosine phosphatase 、 Biology 、 Phosphorylation 、 Proto-oncogene tyrosine-protein kinase Src
摘要: Recent studies from this laboratory have identified novel cytoskeletal proteins that are phosphorylated on tyrosine in vivo Rous sarcoma virus-transformed chick fibroblasts (Glenney, J. R., Jr., and Zokas, L. (1989) Cell Biol. 108, 2401-2408). In the present report, phosphorylation of these was examined cells expressing nonmyristylated mutants src not transformed. A good correlation found between transformation a 22-kDa protein. Tyrosine protein reduced more than 95% src. Size fractionation revealed phosphoprotein transformed is Mr 150,000 complex. Monoclonal antibodies were used to screen various chicken tissues where at high levels muscle lung with low epithelial brain. The becomes an excellent candidate for mediator by kinase class oncogenes.