RESEARCH ARTICLE


Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling



Julie Blouin, Philippe Roby, Mathieu Arcand, Lucille Beaudet, Francesco Lipari*
PerkinElmer Bio-discovery, 1744 William Street, Montreal, Quebec, H3J 1R4, Canada


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© Blouin et al.; Licensee Bentham Open

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* Address correspondence to this author at PerkinElmer Bio-discovery, 1744 William Street, Montreal, Quebec, H3J 1R4, Canada; Tel: 514-937-1010 ext: 314; Fax: 514-937-0777; E-mail: francesco.lipari@perkinelmer.com


Abstract

Out of the 90 human protein tyrosine kinases, 81 were assayed with short peptides derived from well-characterized [CDK1(Tyr15), IRS1(Tyr983), and JAK1(Tyr1023)] or generic [polyGlu:Tyr(4:1) and poly-Glu:Ala:Tyr(1:1:1)] substrates. As expected, the CDK1 peptide is a substrate for all Src family kinases. On the other hand, some of the activities are novel and lead to a better understanding of the function of certain kinases. Specifically, the CDK1 peptide is a substrate for many of the Eph family members. Interestingly, profiling of nearly all the human protein tyrosine kinases revealed a distinct pattern of selectivity towards the CDK1 and IRS1 peptides.

Keywords: Peptide substrates, protein-tyrosine kinases.