NDLI: Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.

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Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.

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Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Witte, O. N. Pendergast, A. M. Muller, A. J. Clark, R. Mccormick, F. Havlik, M. H.
Description	Author Affiliation: Pendergast AM ( Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.);
Abstract	Phosphotyrosine cannot be detected on normal human ABL protein-tyrosine kinases, but activated oncogenic forms of the human ABL protein are phosphorylated on tyrosine in vivo. Activation of ABL can occur by substitution of the ABL first exon with breakpoint cluster region (BCR) sequences or by deletion of the noncatalytic SH3 (src homology region 3) domain. An alternative mode for the activation of the ABL kinases is hyperexpression at greater than 500-fold over endogenous levels. This is not a consequence of transphosphorylation of the hyperexpressed ABL molecules. ABL proteins translated in vitro lack phosphotyrosine, but tyrosine kinase activity is uncovered after immunoprecipitation and removal of lysate components. The rates of dephosphorylation of ABL and BCR-ABL fusion protein by phosphotyrosine-specific phosphatases are approximately the same. These combined results indicate that inhibition of ABL activity is reversible and suggest that a cellular component interacts noncovalently with ABL to inhibit its autophosphorylation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein-Tyrosine Kinases Antagonists & Inhibitors Proto-Oncogene Proteins C-abl Metabolism Animals Baculoviridae Genetics DNA Mutational Analysis Enzyme Activation Gene Expression In Vitro Techniques Insects Phosphotyrosine Proto-Oncogene Proteins Proto-Oncogene Proteins C-bcr Recombinant Proteins Reticulocytes Enzymology Structure-Activity Relationship Tyrosine Analogs & Derivatives Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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