Abstract

The basic objective of this research is the elucidation of the mechanism of neoplastic transformation of cells. Special emphasis will be placed on the biochemical analysis of the process of transformation in cells infected with avian sarcoma viruses. The studies will include the determination of subcellular localization of oncogene products, the identification of target host protein(s) whose phosphorylation is critical for cell transformation, and the characterization of changes in the expression of normal cellular genes in the process of transformation. Analysis of the structure and functions of cellular and viral oncogenes and the conditions required for the conversion of the former to the latter will be continued. The basis for tissue specific transformation by some oncogenic viruses will be explored.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
2R01CA014935-14
Application #
3164050
Study Section
Virology Study Section (VR)
Project Start
1976-05-01
Project End
1991-04-30
Budget Start
1986-05-01
Budget End
1987-04-30
Support Year
14
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Rockefeller University
Department
Type
Graduate Schools
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065

  Publications

Stoeckle, M Y; Sugano, S; Hampe, A et al. (1988) 78-kilodalton glucose-regulated protein is induced in Rous sarcoma virus-transformed cells independently of glucose deprivation. Mol Cell Biol 8:2675-80
Hamaguchi, M; Grandori, C; Hanafusa, H (1988) Phosphorylation of cellular proteins in Rous sarcoma virus-infected cells: analysis by use of anti-phosphotyrosine antibodies. Mol Cell Biol 8:3035-42
Sudol, M; Alvarez-Buylla, A; Hanafusa, H (1988) Differential developmental expression of cellular yes and cellular src proteins in cerebellum. Oncogene Res 2:345-55
Wang, L H; Hanafusa, H (1988) Avian sarcoma viruses. Virus Res 9:159-203
Grandori, C; Hanafusa, H (1988) p60c-src is complexed with a cellular protein in subcellular compartments involved in exocytosis. J Cell Biol 107:2125-35
Kornbluth, S; Sudol, M; Hanafusa, H (1987) Association of the polyomavirus middle-T antigen with c-yes protein. Nature 325:171-3
Kornbluth, S; Jove, R; Hanafusa, H (1987) Characterization of avian and viral p60src proteins expressed in yeast. Proc Natl Acad Sci U S A 84:4455-9
Garber, E A; Mayer, B J; Jove, R et al. (1987) Analysis of p60v-src mutants carrying lesions involved in temperature sensitivity. J Virol 61:354-60
Jove, R; Kornbluth, S; Hanafusa, H (1987) Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region. Cell 50:937-43
Calothy, G; Laugier, D; Cross, F R et al. (1987) The membrane-binding domain and myristylation of p60v-src are not essential for stimulation of cell proliferation. J Virol 61:1678-81

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