期刊
SCIENCE
卷 354, 期 6309, 页码 229-232出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf2144
关键词
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资金
- Ellison Medical Foundation [AG-NS-0953-12]
- Amgen scholarship
- Mary Gates scholarship
- NSF [1243710]
- Human Frontier Science Program award [CDA00069/2013]
- European Research Council [ERC-2014-STG 638884 - PhosFunc]
- Fundacion Botin
- Banco Santander
- Spanish government (FEDER) [BFU2015-64437-P, BFU2014-52333-P]
- Catalan government [2014-SGR-599]
Living organisms have evolved protein phosphorylation, a rapid and versatile mechanism that drives signaling and regulates protein function. We report the phosphoproteomes of 18 fungal species and a phylogenetic-based approach to study phosphosite evolution. We observe rapid divergence, with only a small fraction of phosphosites conserved over hundreds of millions of years. Relative to recently acquired phosphosites, ancient sites are enriched at protein interfaces and are more likely to be functionally important, as we show for sites on H2A1 and eIF4E. We also observe a change in phosphorylation motif frequencies and kinase activities that coincides with the whole-genome duplication event. Our results provide an evolutionary history for phosphosites and suggest that rapid evolution of phosphorylation can contribute strongly to phenotypic diversity.
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