PMID: 9188625Jul 1, 1997Paper

pp60c-src binding to polyomavirus middle T-antigen (MT) requires residues 185 to 210 of the MT sequence

Journal of Virology
C E BrewsterS M Dilworth

Abstract

Interaction with the src family of tyrosine kinases is crucial to the transforming action of polyomavirus middle T-antigen (MT). Association with MT activates the tyrosine kinase activity of pp60(c-src) and, through subsequent MT phosphorylation, creates binding sites for signalling molecules whose stimulation culminates in cell transformation. Despite this importance, and many studies, little is known of the mechanisms by which pp60(c-src) binds to MT. We report here isolation of the first MT mutants that disrupt pp60(c-src) binding without affecting the interaction between MT and protein phosphatase 2A (PP2A). Through deletion analysis we established that interaction with pp60(c-src) requires the sequences between amino acids 185 and 210 of MT, but these residues have no effect on PP2A binding. Cells expressing these mutants showed few altered properties, indicating that the PP2A-MT interaction alone has little influence on cell phenotype. Subcellular location of these mutant MT molecules was indistinguishable by immunofluorescence analysis from that of wild-type MT but was altered markedly on loss of PP2A binding. This suggests a possible role for PP2A in specifying subcellular distribution.

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Citations

Aug 24, 1999·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·M L OliveiraM C Sogayar
May 31, 2001·Microbiology and Molecular Biology Reviews : MMBR·K A Gottlieb, L P Villarreal
Dec 26, 2001·Oncogene·N Ichaso, S M Dilworth
Sep 2, 2009·Microbiology and Molecular Biology Reviews : MMBR·Michele M Fluck, Brian S Schaffhausen
Nov 20, 1998·Molecular and Cellular Biology·K P MullaneB Schaffhausen
Jul 15, 2005·Journal of Virology·Kerry A WhalenBrian S Schaffhausen
Sep 1, 1997·Journal of Virology·M SenftenK Ballmer-Hofer
Jun 10, 2009·Seminars in Cancer Biology·Sarah J L AtkinStephen M Dilworth

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