Abstract：
:Polyomavirus-infected cells express three proteins in the early phase of the lytic cycle, the so-called tumor antigens. Two of them, large- and middle-T antigens, are also required for virus-mediated transformation of primary cells, while middle-T alone is sufficient to transform established cells in culture. Cell transformation by middle-T is strictly dependent on the ability of this protein to associate with cellular enzymes like members of the Src family of tyrosine kinases, a phosphatidylinositol 3-kinase, phosphatase 2A and SHC, an adapter protein linking GDP/GTP exchange factors to tyrosine kinase receptors. A carboxy-terminal stretch of 22 hydrophobic amino acids is required for targeting middle-T and associated proteins to cellular membranes. Here we show in an in vitro system that middle-T fusion proteins carrying an amino-terminal hemagglutinin leader sequence are capable to bind to and enter the lumen of dog pancreas microsomes supporting the concept that the carboxy-terminus of middle-T is an authentic membrane-targeting domain. Furthermore, wild-type middle-T, but not a truncated protein lacking the putative membrane anchor, specifically associates with artificial lipid bilayers.
journal_name
Virus Resjournal_title
Virus researchauthors
Hofer U,Wehrle B,Ballmer-Hofer Kdoi
10.1016/0168-1702(94)00092-qsubject
Has Abstractpub_date
1995-02-01 00:00:00pages
169-80issue
2eissn
0168-1702issn
1872-7492pii
016817029400092Qjournal_volume
35pub_type
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