Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling
Julie Blouin, Philippe Roby, Mathieu Arcand, Lucille Beaudet, Francesco Lipari*
Identifiers and Pagination:Year: 2011
First Page: 115
Last Page: 121
Publisher Id: CCGTM-5-115
Article History:Received Date: 25/3/2011
Revision Received Date: 07/6/2011
Acceptance Date: 11/6/2011
Electronic publication date: 22/8/2011
Collection year: 2011
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.
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.