Functional Asymmetry of the Regions Juxtaposed to the MembraneBinding Sequence of Polyomavirus Middle T Antigen

REFERENCES

• Amini, S., V. DeSeau, S. Reddy, D. Shalloway, and J. B. Bolen. 1986. Regulation of pp60c-src synthesis by inducible RNA complementary to c-src RNA in polyomavirus-transformed rat cells. Mol. Cell. Biol. 6: 2305–2316.
   PubMed Web of Science ®Google Scholar
• Anderson, R. A., and V. T. Marchesi. 1981. Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature (London) 318: 295–298.
   Google Scholar
• Auger, K. R., L. A. Senmian, S. P. Soltoff, P. Libby, and L. C. Cantley. 1989. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell 57: 167–175.
   PubMed Web of Science ®Google Scholar
• Ballmer-Hofer, K., G. Mandel, D. V. Faller, T. M. Roberts, and T. L. Benjamin. 1987. Expression of influenza hemagglutininpolyoma T-antigen fusion proteins in rat embryo fibroblast cell line. Virus Res. 6: 345–361.
   PubMedGoogle Scholar
• Bansal, A., and L. M. Gierasch. 1991. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell 67: 1195–1201.
   PubMedGoogle Scholar
• Benjamin, T. L. 1982. The hr-t gene of polyoma virus. Biochim. Biophys. Acta 695: 69–95.
   PubMedGoogle Scholar
• Bjorge, J. D., T. Chan, M. Antczak, H. Kung, and D. J. Fujita. 1990. Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation. Proc. Natl. Acad. Sci. USA 87: 3816–3820.
   PubMed Web of Science ®Google Scholar
• Bolen, J. B., and M. A. Israel. 1985. Middle tumor antigen of polyomavirus transformation-defective mutant NG59 is associated with pp60c crc. J. Virol. 53: 114–119.
   PubMedGoogle Scholar
• Bolen, J. B., C. J. Thiele, M. A. Israel, W. Yonemoto, L. A. Lipsich, and J. S. Brugge. 1984. Enhancement of cellular src gene product associated tyrosine kinase activity following polyoma virus infection and transformation. Cell 38: 767–777.
   PubMed Web of Science ®Google Scholar
• Brugge, J., E. Erikson, and R. L. Erikson. 1981. The specific interaction of the Rous sarcoma virus transforming protein,pp60c src with two cellular proteins. Cell 25: 363–372.
   PubMed Web of Science ®Google Scholar
• Brugge, J., W. Yonemoto, and D. Darrow. 1983. Interaction between the Rous sarcoma virus transferring protein and two cellular phosphoproteins: analysis of the turnover and distribution of the complex. Mol. Cell. Biol. 3: 9–19.
   PubMed Web of Science ®Google Scholar
• Carmichael, G. G., B. S. Schaffhausen, D. Dorsky, D. Oliver, and T. L. Benjamin. 1982. Carboxy terminus of polyoma middle-sized tumor antigen is required for attachment to membranes, associated protein kinase activities and cell transformation. Proc. Natl. Acad. Sci. USA 79: 3579–3583.
   PubMedGoogle Scholar
• Carmichael, G., B. S. Schaffhausen, G. Mandel, T. J. Liang, and T. L. Benjamin. 1982. Transformation by polyoma virus is drastically reduced by substitution of phenylalanine for tyrosine at residue 315 of middle-sized tumor antigen. Proc. Natl. Acad. Sci. USA 81: 679–683.
   Google Scholar
• Cartwright, C. A., W. Eckhart, S. Simon, and P. L. Kaplan. 1987. Cell transformation by pp60c-src mutated in the carboxy terminal regulatory domain. Cell 49: 83–91.
   PubMed Web of Science ®Google Scholar
• Cepko, C. L., B. E. Roberts, and R. C. Mulligan. 1984. Construction and applications of a highly transmissible murine retrovirus shuttle vector. Cell 37: 1053–1062.
   PubMed Web of Science ®Google Scholar
• Chen, W.-J., J. L. Goldstein, and M. S. Brown. 1990. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265: 3116–3123.
   PubMed Web of Science ®Google Scholar
• Cook, D. N., and J. A. Hassell. 1990. The amino terminus of polyomavirus middle T antigen is required for transformation. J. Virol. 64: 1879–1887.
   PubMedGoogle Scholar
• Courtneidge, S. A. 1985. Activation of the pp60c-src kinase by middle T antigen binding or by dephosphorylation. EMBO J. 4: 1471–1477.
   PubMedGoogle Scholar
• Courtneidge, S. A., and A. Heber. 1987. An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase. Cell 50: 1031–1037.
   PubMed Web of Science ®Google Scholar
• Courtneidge, S. A., and A. E. Smith. 1983. Polyoma virus transforming protein associates with the product of the c-src cellular gene. Nature (London) 303: 435–439.
   PubMed Web of Science ®Google Scholar
• Courtneidge, S. A., and A. E. Smith. 1984. The complex of polyoma virus middle-T antigen and pp60c-src. EMBO J. 3: 585–591.
   PubMedGoogle Scholar
• Cowie, A., J. de Villiers, and R. Kamen. 1986. Immortalization of rat embryo fibroblasts by mutant polyomavirus large T antigen deficient in DNA binding. Mol. Cell. Biol. 6: 4344–4352.
   PubMed Web of Science ®Google Scholar
• Dalbey, R. E. 1990. Positively charged residues are important determinants of membrane protein topology trends. Trends Biochem. Sci. 15: 253–257.
   PubMedGoogle Scholar
• Druker, B. J., L. E. Ling, B. Cohen, T. M. Roberts, and B. S. Schaffhausen. 1990. A completely transformation-defective point mutant of polyomavirus middle T antigen which retains full associated phosphatidylinositol kinase activity. J. Virol. 64: 4454–4461.
   PubMedGoogle Scholar
• Fluck, M., and T. L. Benjamin. 1979. Comparison of two early gene functions essential for transformation in polyoma virus and SV40. Virology 96: 205–228.
   PubMed Web of Science ®Google Scholar
• Freund, R., A. Sotnikov, R. T. Bronson, and T. L. Benjamin. Virology, in press.
   Google Scholar
• Fukui, Y., and H. Hanafiisa. 1989. Phosphatidylinositol kinase activity associates with viral pp60src protein. Mol. Cell. Biol. 9: 1651–1658.
   PubMedGoogle Scholar
• Fukui, Y., S. Kornbluth, S.-M. Jong, L.-H. Wang, and H. Hanafusa. 1989. Phosphatidylinositol kinase type I activity associates with various oncogene products. Oncogene Res. 4: 283–292.
   PubMedGoogle Scholar
• Hirai, H., and H. E. Varmus. 1990. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of pp60c-src. Mol. Cell. Biol. 10: 1307–1318.
   PubMed Web of Science ®Google Scholar
• Kaplan, D. R., M. Whitman, B. S. Schaffhausen, L. Raptis, R. L. Garcea, D. Pallas, T. M. Roberts, and L. Cantley. 1986. Phosphatidylinositol metabolism and polyoma-mediated transformation. Proc. Natl. Acad. Sci. USA 83: 3624–3628.
   PubMedGoogle Scholar
• Kaplan, P. L., S. Simon, C. A. Cartwright, and W. Eckhart. 1987. cDNA cloning with a retrovirus expression vector: generation of a pp60c-src cDNA clone. J. Virol. 61: 1731–1734.
   PubMedGoogle Scholar
• Liang, T. J., G. G. Carmichael, and T. L. Benjamin. 1984. A polyoma mutant that encodes small T antigen but not middle T antigen demonstrates uncoupling of cell surface and cytoskele- tal changes associated with cell transformation. Mol. Cell. Biol. 4: 2774–2783.
   PubMedGoogle Scholar
• Lipsich, L. A., A. J. Lewis, and J. S. Brugge. 1983. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48: 353–360.
   Google Scholar
• Markland, W., S. H. Cheng, B. A. Oostra, and A. E. Smith. 1986. In vitro mutagenesis of the putative membrane-binding domain of polyomavirus middle-T antigen. J. Virol. 59: 82–89.
   PubMedGoogle Scholar
• Markland, W., B. A. Oostra, R. Harvey, A. F. Markham, W. H. Colledge, and A. E. Smith. 1986. Site-directed mutagenesis of polyomavirus middle-T antigen sequences encoding tyrosine 315 and tyrosine 250. J. Virol. 59: 384–391.
   PubMedGoogle Scholar
• Nemeth, S. P., L. G. Fox, M. DeMarco, and J. S. Brugge. 1989. Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein. Mol. Cell. Biol. 9: 1109–1119.
   PubMed Web of Science ®Google Scholar
• Novak, U., and B. E. Griffin. 1981. Requirement for the C-terminal region of middle T-antigen in cellular transformation by polyoma virus. Nucleic Acids Res. 9: 2055–2073.
   PubMed Web of Science ®Google Scholar
• Otsu, M., I. Hiles, I. Gout, M. J. Fry, F. Ruiz-Larrea, G. Panayotou, A. Thompson, R. Dhand, J. Hsuan, N. Totty, A. D. Smith, S. J. Morgan, S. A. Courtneidge, P. J. Parker, and M. D. Waterfield. 1991. Characterization of two 85 kd proteins that associate with receptor tyrosone kinases, middle-T/pp60c-src complexes, and PI3-kinase. Cell 65: 91–104.
   PubMed Web of Science ®Google Scholar
• Pallas, D. C., W. Morgan, and T. M. Roberts. 1989. The cellular proteins which can associate specifically with polyomavirus middle T antigen in human 293 cells include the major human 70-kilodalton heat shock proteins. J. Virol. 63: 4533–4539.
   PubMedGoogle Scholar
• Pallas, D. C., C. Schley, M. Mahoney, E. Harlow, B. S. Schaffhausen, and T. M. Roberts. 1986. Polyomavirus small t antigen: overproduction in bacteria, purification, and utilization for monoclonal and polyclonal antibody production. J. Virol. 60: 1075–1084.
   PubMedGoogle Scholar
• Pallas, D. C., L. K. Shahrik, B. L. Martin, S. Jaspers, T. B. Miller, D. L. Brautigan, and T. M. Roberts. 1990. Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A. Cell 60: 167–176.
   PubMed Web of Science ®Google Scholar
• Pignataro, O. P., and M. Ascoli. 1990. Epidermal growth factor increases the labeling of phosphatidylinositol 3,4-bisphosphate in MA-10 Leydig tumor cells. J. Biol. Chem. 265: 1718–1723.
   PubMed Web of Science ®Google Scholar
• Raptis, L., H. Lamfrom, and T. L. Benjamin. 1985. Regulation of cellular phenotype and expression of polyomavirus middle T antigen in rat fibroblasts. Mol. Cell. Biol. 5: 2476–2485.
   PubMedGoogle Scholar
• Richardson, W. D., B. L. Roberts, and A. E. Smith. 1986. Nuclear location signals in polyoma virus large-T. Cell 44: 77–85.
   PubMedGoogle Scholar
• Ruderman, N. B., R. Kapeller, M. F. White, and L. C. Cantley. 1990. Activation of phosphatidylinositol 3-kinase by insulin. Proc. Natl. Acad. Sci. USA 87: 1411–1415.
   PubMed Web of Science ®Google Scholar
• Schaffhausen, B., and T. L. Benjamin. 1981. Comparison of phosphorylation of two polyoma virus middle T antigens in vivo and in vitro. J. Virol. 40: 184–196.
   PubMed Web of Science ®Google Scholar
• Schaffhausen, B. S., H. Dorai, G. Arakere, and T. L. Benjamin. 1982. Polyoma virus middle T antigen: relationship to cell membranes and apparent lack of ATP-binding activity. Mol. Cell. Biol. 2: 1187–1198.
   PubMedGoogle Scholar
• Schaffhausen, B. S., J. E. Silver, and T. L. Benjamin. 1978. Tumor antigen(s) in cells productively infected by wild-type polyoma virus and mutant NG-18. Proc. Natl. Acad. Sci. USA 75: 79–83.
   PubMed Web of Science ®Google Scholar
• Shibasaki, F., Y. Homma, and T. Takenawa. 1991. Two types of phosphatidylinositol 3-kinase from bovine thymus, monomer and heterodimer forms. J. Biol. Chem. 266: 8108–8114.
   PubMedGoogle Scholar
• Silver, J. E., B. S. Schaffhausen, and T. L. Benjamin. 1978. Tumor antigens induced by nontransforming mutants of polyoma virus. Cell 15: 485–496.
   PubMed Web of Science ®Google Scholar
• Talmage, D. A., R. Freund, A. T. Young, J. Dahl, C. J. Dawe, and T. L. Benjamin. 1989. Phosphorylation of middle T by pp60c-src: a switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis. Cell 59: 55–65.
   PubMed Web of Science ®Google Scholar
• Talmage, D. A., C. Riney, and T. L. Benjamin. 1991. Regulation of pp60c-src expression in rat and mouse fibroblasts by an inducible antisense gene: effects on serum regulation of growth and polyoma virus middle T function. Cell Growth Differ. 2: 51–58.
   PubMedGoogle Scholar
• Templeton, D., and W. Eckhart. 1984. Characterization of viable mutants of polyomavirus cold sensitive for maintenance of cell transformation. J. Virol. 49: 799–805.
   PubMedGoogle Scholar
• Templeton, D., A. Voronova, and W. Eckhart. 1984. Construction and expression of a recombinant DNA gene encoding a polyomavirus middle-size tumor antigen with the carboxyl terminus of the vesicular stomatitis virus glycoprotein G. Mol. Cell. Biol. 4: 282–289.
   PubMedGoogle Scholar
• Treisman, R., U. Novak, J. Favaloro, and R. Kamen. 1981. Transformation of rat cells by an altered polyoma virus genome expressing only the middle T protein. Nature (London) 292: 595–600.
   PubMed Web of Science ®Google Scholar
• Varticorski, L., G. Q. Daley, P. Jackson, D. Baltimore, and L. C. Cantley. 1991. Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants. Mol. Cell. Biol. 11: 1107–1113.
   PubMedGoogle Scholar
• Varticorski, L., B. Druker, D. Morrison, L. Cantley, and T. Roberts. 1989. CSF-1 receptor associates with and activates phosphatidylinositol 3-kinase. Nature (London) 342: 699–702.
   PubMedGoogle Scholar
• Walter, G., A. Carbone, and W. J. Welch. 1987. Medium tumor antigen of polyomavirus transformation-defective mutant NG-59 is associated with 73-kilodalton heat shock protein. J. Virol. 61: 405–410.
   PubMed Web of Science ®Google Scholar
• Walter, G., R. Ruediger, C. Slaughter, and M. Mumby. 1990. Association of protein phosphatase 2A with polyoma virus medium tumor antigen. Proc. Natl. Acad. Sci. USA 87: 2521–2525.
   PubMed Web of Science ®Google Scholar
• Whitman, M., C. P. Downes, M. Keeler, T. Keller, and L. Cantley. 1988. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature (London) 332: 644–646.
   PubMed Web of Science ®Google Scholar
• Whitman, M., D. R. Kaplan, T. M. Roberts, and L. Cantley. 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Biochem. J. 247: 165–174.
   PubMed Web of Science ®Google Scholar
• Whitman, M., D. R. Kaplan, B. S. Schaffhausen, L. Cantley, and T. M. Roberts. 1985. Association of phosphatidylinositol kinase activity with polyoma middle T competent for transformation. Nature (London) 315: 239–242.
   PubMed Web of Science ®Google Scholar