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Gene Review

HpVgp2  -  middle T antigen

Hamster polyomavirus

 
 
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Disease relevance of HpVgp2

 

High impact information on HpVgp2

  • The phosphorylation of proteins on tyrosine in vivo and in vitro was examined in 3T3 cells stimulated by platelet-derived growth factor (PDGF) and transformed by polyoma middle T antigen (MTAg) by using an antibody directed against phosphotyrosine (P-tyr) [6].
  • Expression of the middle-T antigen of polyomavirus is sufficient to induce transformation of fibroblasts in culture and tumour formation in whole animals [7].
  • This growth disturbance was correlated with elevated expression of the PyV middle T antigen and the activation of the PyV middle T antigen-associated c-Yes tyrosine kinase [2].
  • Taken together, these findings suggest that c-Src tyrosine kinase activity is required for PyV middle T antigen-induced mammary tumorigenesis and also illustrate an in vivo genetic approach to the dissection of mitogenic signal transduction pathways [2].
  • Since it is the purpose of this review to consider the natural function of middle T antigen (MT), encoded by one of the seemingly crucial transforming genes of polyomavirus, we will reconsider and redefine the virus and its MT gene in the context of its natural biology and function [8].
 

Chemical compound and disease context of HpVgp2

 

Biological context of HpVgp2

  • Cloned polyomavirus genomes encoding the small T antigen or truncated forms of the middle T antigen facilitated the growth of genomes encoding only the large T antigen in mouse 3T6 cells [14].
  • We have obtained antibodies specific for the polyoma virus middle-size tumor antigen (middle T antigen) by immunizing rabbits with a synthetic peptide, Lys-Arg-Ser-Arg-His-Phe, corresponding to the six carboxy-terminal amino acids of the middle T antigen predicted from the nucleotide sequence of polyoma DNA [15].
  • Polyoma middle T antigen requires cooperation from another gene to express the malignant phenotype in vivo [16].
  • Plasmids expressing partial adenovirus early region 1A (E1A) coding sequences were tested for activities which facilitate in vitro establishment (immortalization) of primary baby rat kidney cells and which enable the T24 Harvey ras-related oncogene and the polyomavirus middle T antigen (pmt) gene to transform primary baby rat kidney cells [17].
  • The effect of mammary gland-specific expression of the polyomavirus middle T antigen was examined by establishing lines of transgenic mice that carry the middle T oncogene under the transcriptional control of the mouse mammary tumor virus promoter/enhancer [18].
 

Anatomical context of HpVgp2

 

Associations of HpVgp2 with chemical compounds

  • This suggests that the association of protein phosphatase 2A with middle T antigen may function to activate PtdIns 3-kinase [23].
  • Experiments with ATP affinity reagents 8-azido-ATP and 2,3-dialdehyde ATP have failed to label the middle T antigen [24].
  • Sucrose gradient fractionation revealed that the middle T antigen was associated with complexes with molecular weights of 500,000 to 1,000,000 [4].
  • Further genetic dissection of this mutant reveals that substituting leucine for proline at amino acid 248 results in a completely transformation defective MTAg [25].
  • At this time, expression of middle-T antigen resulted in the redistribution of shc and src to a brefeldin A resistant perinuclear compartment coincident with the formation of kinase active complexes containing middle-T antigen, shc and src [26].
 

Analytical, diagnostic and therapeutic context of HpVgp2

References

  1. Properties of cells transformed by the middle T-antigen-coding region of polyomavirus. Priehs, C., Friderici, K., Winberry, L., Fluck, M.M. J. Virol. (1986) [Pubmed]
  2. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Guy, C.T., Muthuswamy, S.K., Cardiff, R.D., Soriano, P., Muller, W.J. Genes Dev. (1994) [Pubmed]
  3. ShcA and Grb2 mediate polyoma middle T antigen-induced endothelial transformation and Gab1 tyrosine phosphorylation. Ong, S.H., Dilworth, S., Hauck-Schmalenberger, I., Pawson, T., Kiefer, F. EMBO J. (2001) [Pubmed]
  4. Evidence that the middle T antigen of polyomavirus interacts with the membrane skeleton. Andrews, D.W., Gupta, J., Abisdris, G. Mol. Cell. Biol. (1993) [Pubmed]
  5. Transformation of chicken embryo fibroblasts and tumor induction by the middle T antigen of polyomavirus carried in an avian retroviral vector. Kornbluth, S., Cross, F.R., Harbison, M., Hanafusa, H. Mol. Cell. Biol. (1986) [Pubmed]
  6. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Kaplan, D.R., Whitman, M., Schaffhausen, B., Pallas, D.C., White, M., Cantley, L., Roberts, T.M. Cell (1987) [Pubmed]
  7. Association of the polyomavirus middle-T antigen with c-yes protein. Kornbluth, S., Sudol, M., Hanafusa, H. Nature (1987) [Pubmed]
  8. Natural biology of polyomavirus middle T antigen. Gottlieb, K.A., Villarreal, L.P. Microbiol. Mol. Biol. Rev. (2001) [Pubmed]
  9. Identification of the threonine phosphorylation sites on the polyomavirus major capsid protein VP1: relationship to the activity of middle T antigen. Li, M., Garcea, R.L. J. Virol. (1994) [Pubmed]
  10. Serine 257 phosphorylation regulates association of polyomavirus middle T antigen with 14-3-3 proteins. Culleré, X., Rose, P., Thathamangalam, U., Chatterjee, A., Mullane, K.P., Pallas, D.C., Benjamin, T.L., Roberts, T.M., Schaffhausen, B.S. J. Virol. (1998) [Pubmed]
  11. Phosphatidylinositol metabolism in cells transformed by polyomavirus middle T antigen. Ulug, E.T., Hawkins, P.T., Hanley, M.R., Courtneidge, S.A. J. Virol. (1990) [Pubmed]
  12. 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. Glenn, G.M., Eckhart, W. J. Virol. (1993) [Pubmed]
  13. Inhibition of pp60c-src protein kinase by herbimycin A in polyomavirus middle tumor antigen-transformed cells. Yang, Y.W., Chang, Y.H. Anticancer Res. (1997) [Pubmed]
  14. Truncated forms of the polyomavirus middle T antigen can substitute for the small T antigen in lytic infection. Templeton, D., Simon, S., Eckhart, W. J. Virol. (1986) [Pubmed]
  15. Antibodies specific for the polyoma virus middle-size tumor antigen. Walter, G., Hutchinson, M.A., Hunter, T., Eckhart, W. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  16. Polyoma middle T antigen requires cooperation from another gene to express the malignant phenotype in vivo. Asselin, C., Gélinas, C., Branton, P.E., Bastin, M. Mol. Cell. Biol. (1984) [Pubmed]
  17. Adenovirus E1A coding sequences that enable ras and pmt oncogenes to transform cultured primary cells. Zerler, B., Moran, B., Maruyama, K., Moomaw, J., Grodzicker, T., Ruley, H.E. Mol. Cell. Biol. (1986) [Pubmed]
  18. Induction of mammary tumors by expression of polyomavirus middle T oncogene: a transgenic mouse model for metastatic disease. Guy, C.T., Cardiff, R.D., Muller, W.J. Mol. Cell. Biol. (1992) [Pubmed]
  19. Phosphorylation of polyoma middle T antigen and cellular proteins in purified plasma membranes of polyoma virus-infected cells. Ballmer-Hofer, K., Benjamin, T.L. EMBO J. (1985) [Pubmed]
  20. Polyoma middle T-induced vascular tumor formation: the role of the plasminogen activator/plasmin system. Sabapathy, K.T., Pepper, M.S., Kiefer, F., Möhle-Steinlein, U., Tacchini-Cottier, F., Fetka, I., Breier, G., Risau, W., Carmeliet, P., Montesano, R., Wagner, E.F. J. Cell Biol. (1997) [Pubmed]
  21. Cooperation between the polyomavirus middle-T-antigen gene and the human c-myc oncogene in a rat thyroid epithelial differentiated cell line: model of in vitro progression. Berlingieri, M.T., Portella, G., Grieco, M., Santoro, M., Fusco, A. Mol. Cell. Biol. (1988) [Pubmed]
  22. Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression. Hutchinson, J., Jin, J., Cardiff, R.D., Woodgett, J.R., Muller, W.J. Mol. Cell. Biol. (2001) [Pubmed]
  23. A tightly associated serine/threonine protein kinase regulates phosphoinositide 3-kinase activity. Carpenter, C.L., Auger, K.R., Duckworth, B.C., Hou, W.M., Schaffhausen, B., Cantley, L.C. Mol. Cell. Biol. (1993) [Pubmed]
  24. Polyoma virus middle T antigen: relationship to cell membranes and apparent lack of ATP-binding activity. Schaffhausen, B.S., Dorai, H., Arakere, G., Benjamin, T.L. Mol. Cell. Biol. (1982) [Pubmed]
  25. Generation of a large library of point mutations in polyoma middle T antigen. Druker, B.J., Roberts, T.M. Nucleic Acids Res. (1991) [Pubmed]
  26. At the onset of transformation polyomavirus middle-T recruits shc and src to a perinuclear compartment coincident with condensation of endosomes. Zhu, W., Eicher, A., Leber, B., Andrews, D.W. Oncogene (1998) [Pubmed]
  27. The Septin 9 (MSF) gene is amplified and overexpressed in mouse mammary gland adenocarcinomas and human breast cancer cell lines. Montagna, C., Lyu, M.S., Hunter, K., Lukes, L., Lowther, W., Reppert, T., Hissong, B., Weaver, Z., Ried, T. Cancer Res. (2003) [Pubmed]
  28. Cell fractionation in non-ionic detergent distinguishes sub-populations of polyoma virus middle T antigen and reveals a novel form. Krauzewicz, N., Elliott, J., Griffin, B.E. Oncogene (1994) [Pubmed]
  29. Site-directed mutagenesis of polyomavirus middle-T antigen sequences encoding tyrosine 315 and tyrosine 250. Markland, W., Oostra, B.A., Harvey, R., Markham, A.F., Colledge, W.H., Smith, A.E. J. Virol. (1986) [Pubmed]
  30. A completely transformation-defective point mutant of polyomavirus middle T antigen which retains full associated phosphatidylinositol kinase activity. Druker, B.J., Ling, L.E., Cohen, B., Roberts, T.M., Schaffhausen, B.S. J. Virol. (1990) [Pubmed]
  31. A transgenic mouse line harboring a smooth muscle alpha-actin promoter polyomavirus middle T antigen transgene develops an epithelial hyperplasia in the rectum and distal stomach. Moghal, N., Bonyadi, S., Hassell, J.A., Alpert, L., Chalifour, L.E. Lab. Invest. (1995) [Pubmed]
 
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