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In vitro substrate specificity of protein tyrosine kinases

  • Protein Kinases
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Abstract

Synthetic peptides such as P60stc autophosphorylation site peptides and angiotensin are indiscriminately phosphorylated by protein tyrosine kinases. The observation has led to the general belief that protein tyrosine kinases are highly promiscuous, displaying littlein vitro site specificity. In recent years, evidence has been accumulating to indicate that such a belief requires close examination. Synthetic peptides showing high substrate activity for specific groups of protein tyrosine kinases have been obtained. Systematic modification of certain substrate peptides suggests that kinase substrate determinants reside with specific amino acid residues proximal to the target tyrosine. A number of protein kinases have been shown to be regulated by tyrosine phosphorylation at specific sites by highly specific protein tyrosine kinases. These and other selected biochemical studies that contribute to the evolving view ofin vitro substrate specificity of protein tyrosine kinases are reviewed.

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Authors and Affiliations

  1. Department of Medical Biochemistry, MRC Group in Signal Transduction, The University of Calgary, T2N 4N1, Calgary, Alberta, Canada

    Isao Matsuura & Jerry H. Wang

  2. Russell Grimwade School of Biochemistry, University of Melbourne, 3052, Parkville, Victoria, Australia

    Heung-Chin Cheng

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  1. Heung-Chin Cheng
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  2. Isao Matsuura
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  3. Jerry H. Wang
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Cheng, HC., Matsuura, I. & Wang, J.H. In vitro substrate specificity of protein tyrosine kinases. Mol Cell Biochem 127, 103–112 (1993). https://doi.org/10.1007/BF01076761

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