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Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling
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 kinas...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Bentham Open
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178905/ https://www.ncbi.nlm.nih.gov/pubmed/21966344 http://dx.doi.org/10.2174/1875397301105010115 |
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author | Blouin, Julie Roby, Philippe Arcand, Mathieu Beaudet, Lucille Lipari, Francesco |
author_facet | Blouin, Julie Roby, Philippe Arcand, Mathieu Beaudet, Lucille Lipari, Francesco |
author_sort | Blouin, Julie |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3178905 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Bentham Open |
record_format | MEDLINE/PubMed |
spelling | pubmed-31789052011-09-30 Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling Blouin, Julie Roby, Philippe Arcand, Mathieu Beaudet, Lucille Lipari, Francesco Curr Chem Genomics Article 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. Bentham Open 2011-08-22 /pmc/articles/PMC3178905/ /pubmed/21966344 http://dx.doi.org/10.2174/1875397301105010115 Text en © Blouin et al.; Licensee Bentham Open http://creativecommons.org/licenses/by-nc/3.0/ 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. |
spellingShingle | Article Blouin, Julie Roby, Philippe Arcand, Mathieu Beaudet, Lucille Lipari, Francesco Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title | Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title_full | Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title_fullStr | Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title_full_unstemmed | Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title_short | Catalytic Specificity of Human Protein Tyrosine Kinases Revealed by Peptide Substrate Profiling |
title_sort | catalytic specificity of human protein tyrosine kinases revealed by peptide substrate profiling |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178905/ https://www.ncbi.nlm.nih.gov/pubmed/21966344 http://dx.doi.org/10.2174/1875397301105010115 |
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