Literature DB >> 6304524

Polyoma virus transforming protein associates with the product of the c-src cellular gene.

S A Courtneidge, A E Smith.   

Abstract

Polyoma virus can transform the growth properties of rodent cells grown in culture and form tumours in susceptible animals, an activity largely due to one of the virus-encoded proteins, called middle T. Middle T has an associated tyrosine-specific protein kinase activity in vitro and interacts with cellular membranes, but the biochemical basis of its ability to transform remains unclear. Although there is some correlation between the transforming activity of different polyoma virus mutants and their ability to accept phosphate on tyrosine in middle T in the in vitro kinase reaction, the abundance of phosphotyrosine in protein is not elevated in polyoma virus-transformed cells and no cellular substrates for the putative kinase have been identified. It is also not yet known whether the tyrosine kinase of middle T is an intrinsic activity of the protein itself or the property of an associated enzyme. The experiments described here indicate that a fraction of middle T forms a stable complex with pp60c-src, the product of a cellular oncogene, and lead us to propose that the middle T associated kinase at least in part is a property of pp60c-src rather than middle T itself.

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Year:  1983        PMID: 6304524     DOI: 10.1038/303435a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  231 in total

Review 1.  Natural biology of polyomavirus middle T antigen.

Authors:  K A Gottlieb; L P Villarreal
Journal:  Microbiol Mol Biol Rev       Date:  2001-06       Impact factor: 11.056

2.  The collagen repeat sequence is a determinant of the degree of herpesvirus saimiri STP transforming activity.

Authors:  J K Choi; S Ishido; J U Jung
Journal:  J Virol       Date:  2000-09       Impact factor: 5.103

3.  The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little resemblance to T antigens.

Authors:  D C Pallas; W Weller; S Jaspers; T B Miller; W S Lane; T M Roberts
Journal:  J Virol       Date:  1992-02       Impact factor: 5.103

4.  Characterization of the interaction of polyomavirus middle T antigen with type 2A protein phosphatase.

Authors:  E T Ulug; A J Cartwright; S A Courtneidge
Journal:  J Virol       Date:  1992-03       Impact factor: 5.103

5.  Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells.

Authors:  L Petti; D DiMaio
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-01       Impact factor: 11.205

6.  An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases.

Authors:  A L Burkhardt; J B Bolen; E Kieff; R Longnecker
Journal:  J Virol       Date:  1992-08       Impact factor: 5.103

7.  Interactions of polyomavirus middle T with the SH2 domains of the pp85 subunit of phosphatidylinositol-3-kinase.

Authors:  M Yoakim; W Hou; Y Liu; C L Carpenter; R Kapeller; B S Schaffhausen
Journal:  J Virol       Date:  1992-09       Impact factor: 5.103

Review 8.  Regulation of renal function and structure by the signaling Na/K-ATPase.

Authors:  Jeffrey X Xie; Xin Li; Zijian Xie
Journal:  IUBMB Life       Date:  2013-12-10       Impact factor: 3.885

9.  Phosphorylation in vitro of Escherichia coli-produced 235R and 266R tumor antigens encoded by human adenovirus type 12 early transformation region 1A.

Authors:  L A Lucher; P M Loewenstein; M Green
Journal:  J Virol       Date:  1985-10       Impact factor: 5.103

10.  Mutation of a cysteine residue in polyomavirus middle T antigen abolishes interactions with protein phosphatase 2A, pp60c-src, and phosphatidylinositol-3 kinase, activation of c-fos expression, and cellular transformation.

Authors:  G M Glenn; W Eckhart
Journal:  J Virol       Date:  1993-04       Impact factor: 5.103

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