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Authors: Genie C Leung James M Murphy Doug Briant Frank Sicheri
Publish Date: 2009
Volume: , Issue: , Pages: 187-195
Abstract
The human proteome is known to contain 500 protein kinases which regulate almost all facets of cellular biology by the posttranslational attachment of a phosphate moiety to serine threonine or tyrosine residues within a substrate protein Most protein kinases remain poorly characterized and as a result current studies are directed toward defining their target substrates experimentally to gain a comprehensive view of the signaling proteins and pathways modulated by these kinases Herein we describe a rapid and convenient method for elucidating the consensus substrate motif for phosphorylation by a protein kinase using peptide SPOT arrays that are customsynthesized on a cellulose membrane support The definition of the target consensus motif provides an important starting point for the identification of physiologically relevant kinase substratesWe thank CS Ho and IM Blasutig for helpful comments on the manuscript and T Pawson for use of his Multipep SPOT synthesizer This work was supported by grants from the National Cancer Institute of Canada and the Canadian Institutes of Health Research to FS and from the Terry Fox Foundation through an award from National Cancer Institute of Canada to GCL JMM is a recipient of a CJ Martin Biomedical Fellowship from the National Health and Medical Research Council of Australia
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