
Stoichiometry of cellular and viral components in the polyomavirus middle-T antigen-tyrosine kinase complex.
Author(s) -
Seng H. Cheng,
P. C. Espino,
John Marshall,
R Harvey,
Alan E. Smith
Publication year - 1990
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.10.10.5569
Subject(s) - biology , tyrosine kinase , phosphoprotein , antigen , kinase , tyrosine , platelet derived growth factor receptor , proto oncogene tyrosine protein kinase src , microbiology and biotechnology , cyclin dependent kinase 5 , virology , biochemistry , phosphorylation , signal transduction , mitogen activated protein kinase kinase , protein kinase a , immunology , receptor , growth factor
Our results indicate that only one type of tyrosine kinase is present within each middle-T antigen-tyrosine kinase complex, suggesting that middle-T antigen forms separate complexes with different tyrosine kinases. Furthermore, we determined that there is only one molecule of middle-T antigen within any one of these complexes. We interpret this to mean that in any given cell, polyomavirus transformation involves, at least in part, the simultaneous deregulation of a number of separate pathways controlling cellular proliferation. Finally, we also demonstrate that the separate middle-T:pp60c-src and middle-T:pp59c-fyn complexes are each able to interact with the same cellular p81/85-kDa phosphoprotein, a possible component of the phosphatidylinositol kinase.