Comparative phosphoproteomics reveals evolutionary and functional conservation of phosphorylation across eukaryotes |
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| Authors: | Jos Boekhorst Bas van Breukelen Albert JR Heck Berend Snel |
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| Affiliation: | (1) Bioinformatics, Department of Biology, Faculty of Science, Utrecht University, Padualaan, 3584, CH, The Netherlands;(2) Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan, 3584, CA Utrecht, The Netherlands;(3) Academic Biomedical Centre, Utrecht University, Yalelaan, 3584, CL Utrecht, The Netherlands |
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| Abstract: | Background Reversible phosphorylation of proteins is involved in a wide range of processes, ranging from signaling cascades to regulation of protein complex assembly. Little is known about the structure and evolution of phosphorylation networks. Recent high-throughput phosphoproteomics studies have resulted in the rapid accumulation of phosphopeptide datasets for many model organisms. Here, we exploit these novel data for the comparative analysis of phosphorylation events between different species of eukaryotes. |
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