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Characterization of the TPR-MET Oncogene p65 and the MET Protooncogene p140 Protein-Tyrosine Kinases

M. Gonzatti-Haces, A. Seth, M. Park, T. Copeland, S. Oroszlan and G. F. Vande Woude
Proceedings of the National Academy of Sciences of the United States of America
Vol. 85, No. 1 (Jan. 1, 1988), pp. 21-25
Stable URL: http://www.jstor.org/stable/30998
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Characterization of the TPR-MET Oncogene p65 and the MET Protooncogene p140 Protein-Tyrosine Kinases
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Abstract

The proteins encoded by the human TPR-MET oncogene (p65tpr-met) and the human MET protooncogene (p140met) have been identified. The p65tpr-met and p140met, as well as a truncated TPR-MET product expressed in Escherichia coli, p50met, are autophosphorylated in vitro on tyrosine residues. Using the immunocomplex kinase assay, p140met activity was detected in various human tumor epithelial cell lines. In vivo, p65tpr-met is phosphorylated on both serine and tyrosine residues, while p140met is phosphorylated on serine and threonine. p140met is labeled by cell-surface iodination procedures, suggesting that it is a receptor-like transmembrane protein-tyrosine kinase.

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