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Binding of Transforming Protein, P47 gag-crk , to a Broad Range of Phosphotyrosine-containing Proteins
Abstract
Although the oncogene product of CT10 virus, P47 gag-crk , does not itself phosphorylate proteins at tyrosine residues, it elevates phosphotyrosine in transformed cells. The P47 gag-crk oncoprotein contains SH2 and SH3 domains, which are conserved in several proteins involved in signal transduction, including nonreceptor tyrosine kinases. P47 gag-crk bound in vitro to phosphotyrosine-containing proteins from crk -transformed cells and from cells transformed by oncogenic tyrosine kinases. The association between P47 gag-crk and p60 v- src , a phosphotyrosine-containing protein, was abolished by dephosphorylation of p60 v- src . This suggests that the SH2 and SH3 regions function to regulate protein interactions in a phosphotyrosine-dependent manner.
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Kirsch, K. H., Georgescu, M.-M., Ishimaru, S., & Hanafusa, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6211 · Cited by 162
Self-citationYi, T. L., Cleveland, J. L., & Ihle, J. N. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.836 · Cited by 144
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Metadata
- Authors
- Matsuda, M., Mayer, B. J., Fukui, Y., & Hanafusa, H.
- Venue
- Science
- Published
- 1990-06-22
- Volume
- 248
- Issue
- 4962
- Pages
- 1537-1539
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1979253402
- Cited by
- 411
- References
- 0
- FWCI
- 17.83
- Type
- journal article
- Language
- en
- Open access
- closed
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