Mayer, Bruce J. and Jackson, Peter K. and Baltimore, David (1991) The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proceedings of the National Academy of Sciences of the United States of America, 88 (2). pp. 627-631. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:MAYpnas91
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Several proteins implicated in the regulation of cell proliferation contain a common noncatalytic domain, src homology region 2 (SH2). We have used the bacterially expressed SH2 domain of abl protein-tyrosine kinase to evaluate the ability of this domain to bind to cellular proteins. abl SH2 specifically bound to a number of tyrosine-phosphorylated proteins from cells transformed by tyrosine kinase oncogenes in a filter-binding assay and to a subset of those proteins in solution. The SH2 probe bound almost exclusively to tyrosine-phosphorylated proteins, and binding was eliminated by dephosphorylation of cell proteins. Free phosphotyrosine could partially disrupt SH2 binding, suggesting that phosphotyrosine is directly involved in the binding interaction. These results demonstrate that an SH2 domain is sufficient to confer direct, high-affinity phosphotyrosine-dependant binding to proteins and suggest a general role for SH2 domains in cellular signaling pathways.
|Additional Information:||© 1991 by the National Academy of Sciences. Contributed by David Baltimore, October 4, 1990. We are grateful to H. Hanafusa, M. Matsuda, and T. Pawson for generously discussing unpublished results and thank M. Kamps for anti-ptyr antibody and for critically reading this manuscript. This work was supported by U.S. Public Health Service Grant CA51462 from the National Cancer Institute. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
|Subject Keywords:||phosphoyrosine; signal transduction; transformation; oncogenes|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||08 Nov 2007|
|Last Modified:||26 Dec 2012 09:46|
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