Global Analysis of Cdk1 Substrate Phosphorylation Sites Provides Insights into Evolution Export

@article{citeulike:5838555, abstract = {To explore the mechanisms and evolution of cell-cycle control, we analyzed the position and conservation of large numbers of phosphorylation sites for the cyclin-dependent kinase Cdk1 in the budding yeast Saccharomyces cerevisiae. We combined specific chemical inhibition of Cdk1 with quantitative mass spectrometry to identify the positions of 547 phosphorylation sites on 308 Cdk1 substrates in vivo. Comparisons of these substrates with orthologs throughout the ascomycete lineage revealed that the position of most phosphorylation sites is not conserved in evolution; instead, clusters of sites shift position in rapidly evolving disordered regions. We propose that the regulation of protein function by phosphorylation often depends on simple nonspecific mechanisms that disrupt or enhance protein-protein interactions. The gain or loss of phosphorylation sites in rapidly evolving regions could facilitate the evolution of kinase-signaling circuits. 10.1126/science.1172867}, author = {Holt, Liam J. and Tuch, Brian B. and Villen, Judit and Johnson, Alexander D. and Gygi, Steven P. and Morgan, David O.}, citeulike-article-id = {5838555}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1172867}, citeulike-linkout-1 = {http://www.sciencemag.org/content/325/5948/1682.abstract}, citeulike-linkout-2 = {http://www.sciencemag.org/content/325/5948/1682.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19779198}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19779198}, day = {25}, doi = {10.1126/science.1172867}, issn = {1095-9203}, journal = {Science}, keywords = {analysis, cdk, evolution, kinase, phosphorylation}, month = {September}, number = {5948}, pages = {1682--1686}, posted-at = {2009-09-25 00:17:38}, priority = {2}, title = {Global Analysis of Cdk1 Substrate Phosphorylation Sites Provides Insights into Evolution}, url = {http://dx.doi.org/10.1126/science.1172867}, volume = {325}, year = {2009} }

TY - JOUR ID - citeulike:5838555 L3 - citeulike-article-id:5838555 N2 - To explore the mechanisms and evolution of cell-cycle control, we analyzed the position and conservation of large numbers of phosphorylation sites for the cyclin-dependent kinase Cdk1 in the budding yeast Saccharomyces cerevisiae. We combined specific chemical inhibition of Cdk1 with quantitative mass spectrometry to identify the positions of 547 phosphorylation sites on 308 Cdk1 substrates in vivo. Comparisons of these substrates with orthologs throughout the ascomycete lineage revealed that the position of most phosphorylation sites is not conserved in evolution; instead, clusters of sites shift position in rapidly evolving disordered regions. We propose that the regulation of protein function by phosphorylation often depends on simple nonspecific mechanisms that disrupt or enhance protein-protein interactions. The gain or loss of phosphorylation sites in rapidly evolving regions could facilitate the evolution of kinase-signaling circuits. 10.1126/science.1172867 IS - 5948 JF - Science SN - 1095-9203 EP - 1686 TI - Global Analysis of Cdk1 Substrate Phosphorylation Sites Provides Insights into Evolution VL - 325 SP - 1682 KW - analysis KW - cdk KW - evolution KW - kinase KW - phosphorylation AU - Holt, Liam AU - Tuch, Brian AU - Villen, Judit AU - Johnson, Alexander AU - Gygi, Steven AU - Morgan, David PY - 2009/09/25/ UR - http://dx.doi.org/10.1126/science.1172867 ER -