Evolution of protein phosphorylation across 18 fungal species

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2016-10, Vol.354 (6309), p.229-232
Main Authors: Studer, Romain A., Rodriguez-Mias, Ricard A., Haas, Kelsey M., Hsu, Joanne I., Viéitez, Cristina, Solé, Carme, Swaney, Danielle L., Stanford, Lindsay B., Liachko, Ivan, Böttcher, René, Dunham, Maitreya J., de Nadal, Eulàlia, Posas, Francesc, Beltrao, Pedro, Villén, Judit
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological evolution
Evolution
Evolution, Molecular
Fungal Proteins - classification
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fungi
Fungi - genetics
Fungi - metabolism
Genome, Fungal
Genomics
Historic sites
Kinases
Organisms
Phenotype
Phosphoproteins - classification
Phosphoproteins - genetics
Phosphoproteins - metabolism
Phosphorylation
Phosphorylation - genetics
Phylogeny
Protein Processing, Post-Translational
Protein-Serine-Threonine Kinases - classification
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Proteins
Proteome - genetics
Proteome - metabolism
Reproduction
Signal Transduction
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Summary: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 elF4E. We also observe a change in phosphorylation motif frequencies and kinase activities that coincides with the wholegenome duplication event. Our results provide an evolutionary history for phosphosites and suggest that rapid evolution of phosphorylation can contribute strongly to phenotypic diversity.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.aaf2144