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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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2016-10, Vol.354 (6309), p.229-232 |
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| creator | 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 |
| description | 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. |
| doi_str_mv | 10.1126/science.aaf2144 |
| format | Article |
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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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aaf2144</identifier><identifier>PMID: 27738172</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>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</subject><ispartof>Science (American Association for the Advancement of Science), 2016-10, Vol.354 (6309), p.229-232</ispartof><rights>Copyright © 2016 American Association for the Advancement of Science</rights><rights>Copyright © 2016, American Association for the Advancement of Science.</rights><rights>Copyright © 2016, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-10a24745399bc8c0ad2b3bc4ed11fe952415871f8323d2212551d5a21cab01013</citedby><cites>FETCH-LOGICAL-c520t-10a24745399bc8c0ad2b3bc4ed11fe952415871f8323d2212551d5a21cab01013</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/44710800$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/44710800$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27738172$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Studer, Romain A.</creatorcontrib><creatorcontrib>Rodriguez-Mias, Ricard A.</creatorcontrib><creatorcontrib>Haas, Kelsey M.</creatorcontrib><creatorcontrib>Hsu, Joanne I.</creatorcontrib><creatorcontrib>Viéitez, Cristina</creatorcontrib><creatorcontrib>Solé, Carme</creatorcontrib><creatorcontrib>Swaney, Danielle L.</creatorcontrib><creatorcontrib>Stanford, Lindsay B.</creatorcontrib><creatorcontrib>Liachko, Ivan</creatorcontrib><creatorcontrib>Böttcher, René</creatorcontrib><creatorcontrib>Dunham, Maitreya J.</creatorcontrib><creatorcontrib>de Nadal, Eulàlia</creatorcontrib><creatorcontrib>Posas, Francesc</creatorcontrib><creatorcontrib>Beltrao, Pedro</creatorcontrib><creatorcontrib>Villén, Judit</creatorcontrib><title>Evolution of protein phosphorylation across 18 fungal species</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Biological evolution</subject><subject>Evolution</subject><subject>Evolution, Molecular</subject><subject>Fungal Proteins - classification</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Fungi - genetics</subject><subject>Fungi - metabolism</subject><subject>Genome, Fungal</subject><subject>Genomics</subject><subject>Historic sites</subject><subject>Kinases</subject><subject>Organisms</subject><subject>Phenotype</subject><subject>Phosphoproteins - classification</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphorylation - genetics</subject><subject>Phylogeny</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein-Serine-Threonine Kinases - 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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.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>27738172</pmid><doi>10.1126/science.aaf2144</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| 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 |
| title | Evolution of protein phosphorylation across 18 fungal species |
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