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Sci. Signal., 16 February 2010
Vol. 3, Issue 109, p. ra12
[DOI: 10.1126/scisignal.2000482]


Editor's Summary

Exploring Kinase Selectivity
Kinases are master regulators of cellular behavior. Because of the large number of kinases and the even larger number of substrates, approaches that permit global analysis are valuable tools for investigating kinase biology. Mok et al. identified the phosphorylation site selectivity for 61 of the 122 kinases in Saccharomyces cerevisiae by screening a miniaturized peptide library. By integrating these data with other data sets and structural information, they revealed information about the relationship between kinase catalytic residues and substrate selectivity. They also identified and experimentally verified substrates for kinases, including one for which limited functional information was previously available, showing the potential for this type of analysis as a launching point for the exploration of the biological functions of kinases.

Citation: J. Mok, P. M. Kim, H. Y. K. Lam, S. Piccirillo, X. Zhou, G. R. Jeschke, D. L. Sheridan, S. A. Parker, V. Desai, M. Jwa, E. Cameroni, H. Niu, M. Good, A. Remenyi, J.-L. N. Ma, Y.-J. Sheu, H. E. Sassi, R. Sopko, C. S. M. Chan, C. De Virgilio, N. M. Hollingsworth, W. A. Lim, D. F. Stern, B. Stillman, B. J. Andrews, M. B. Gerstein, M. Snyder, B. E. Turk, Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs. Sci. Signal. 3, ra12 (2010).

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