This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hamaguchi, M
Right arrow Articles by Hanafusa, H
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hamaguchi, M
Right arrow Articles by Hanafusa, H

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 August; 8(8): 3035-3042

Phosphorylation of cellular proteins in Rous sarcoma virus-infected cells: analysis by use of anti-phosphotyrosine antibodies.

M Hamaguchi, C Grandori and H Hanafusa

Rockefeller University, New York, New York 10021.

ABSTRACT

The protein substrates for the tyrosine protein kinases in cells transformed by avian sarcoma viruses were analyzed by gel electrophoresis in combination with immunoblotting or immunoprecipitation by antibodies against phosphotyrosine. We found that greater than 90% of phosphotyrosine-containing cellular proteins can be immunoprecipitated by these antibodies. The level of phosphotyrosine-containing cellular proteins detectable by this method markedly increased upon transformation with Rous sarcoma virus, and more than 20 distinct bands of such proteins were found in lysates of Rous sarcoma virus-transformed cells. Most of these phosphotyrosine-containing proteins had not been identified by other methods, and their presence appeared to correlate with morphological transformation in cells infected with various Rous sarcoma virus mutants and Y73, PRCII, and Fujinami sarcoma viruses. However, considerably different patterns were obtained with cells infected with nontransforming Rous sarcoma virus mutants that encode nonmyristylated src kinases, indicating that most substrates that correlate with transformation can only be recognized by p60v-src associated with the plasma membrane.

Mol Cell Biol. 1988 August; 8(8): 3035-3042




This article has been cited by other articles:

  • Ruhul Amin, A.R.M., Uddin Biswas, M. H., Senga, T., Feng, G.-S., Kannagi, R., Agarwal, M. L., Hamaguchi, M. (2007). A role for SHPS-1/SIRP{alpha} in Concanavalin A-dependent production of MMP-9. GENES CELLS 12: 1023-1033 [Abstract] [Full Text]  
  • Mon, N. N., Hasegawa, H., Thant, A. A., Huang, P., Tanimura, Y., Senga, T., Hamaguchi, M. (2006). A Role for Focal Adhesion Kinase Signaling in Tumor Necrosis Factor-{alpha}-Dependent Matrix Metalloproteinase-9 Production in a Cholangiocarcinoma Cell Line, CCKS1.. Cancer Res. 66: 6778-6784 [Abstract] [Full Text]  
  • Ruhul Amin, A. R. M., Oo, M. L., Senga, T., Suzuki, N., Feng, G.-S., Hamaguchi, M. (2003). SH2 Domain Containing Protein Tyrosine Phosphatase 2 Regulates Concanavalin A-dependent Secretion and Activation of Matrix Metalloproteinase 2 via the Extracellular Signal-regulated Kinase and p38 Pathways. Cancer Res. 63: 6334-6339 [Abstract] [Full Text]  
  • Sohara, Y., Ishiguro, N., Machida, K., Kurata, H., Thant, A. A., Senga, T., Matsuda, S., Kimata, K., Iwata, H., Hamaguchi, M. (2001). Hyaluronan Activates Cell Motility of v-Src-transformed Cells via Ras-Mitogen-activated Protein Kinase and Phosphoinositide 3-Kinase-Akt in a Tumor-specific Manner. Mol. Biol. Cell 12: 1859-1868 [Abstract] [Full Text]  
  • Liu, E., Thant, A. A., Kikkawa, F., Kurata, H., Tanaka, S., Nawa, A., Mizutani, S., Matsuda, S., Hanafusa, H., Hamaguchi, M. (2000). The Ras-Mitogen-activated Protein Kinase Pathway Is Critical for the Activation of Matrix Metalloproteinase Secretion and the Invasiveness in v-crk-transformed 3Y1. Cancer Res. 60: 2361-2364 [Abstract] [Full Text]  
  • Corellou, F, Bisgrove, S., Kropf, D., Meijer, L, Kloareg, B, Bouget, F. (2000). A S/M DNA replication checkpoint prevents nuclear and cytoplasmic events of cell division including centrosomal axis alignment and inhibits activation of cyclin-dependent kinase-like proteins in fucoid zygotes. Development 127: 1651-1660 [Abstract]  
  • Matsuda, S., Katsumata, R., Okuda, T., Yamamoto, T., Miyazaki, K., Senga, T., Machida, K., Thant, A. A., Nakatsugawa, S., Hamaguchi, M. (2000). Molecular Cloning and Characterization of Human MAWD, a Novel Protein Containing WD-40 Repeats Frequently Overexpressed in Breast Cancer. Cancer Res. 60: 13-17 [Abstract] [Full Text]  
  • Yamanashi, Y, Kakiuchi, T, Mizuguchi, J, Yamamoto, T, Toyoshima, K (1991). Association of B cell antigen receptor with protein tyrosine kinase Lyn. Science 251: 192-194 [Abstract]  
  • Matsuda, M, Mayer, B., Fukui, Y, Hanafusa, H (1990). Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248: 1537-1539 [Abstract]  
  • Lugo, T., Pendergast, A., Muller, A., Witte, O. (1990). Tyrosine kinase activity and transformation potency of bcr-abl oncogene products. Science 247: 1079-1082 [Abstract]  
  • Mayer, B.J., Hamaguchi, M., Hanafusa, H. (1988). Characterization of p47gag-crk, a Novel Oncogene Product with Sequence Similarity to a Putative Modulatory Domain of Protein-Tyrosine Kinases and Phospholipase C. Cold Spring Harb Symp Quant Biol 53: 907-914 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»