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Systematic identification of phosphorylation-mediated protein interaction switches

Proteomics techniques can identify thousands of phosphorylation sites in a single experiment, the majority of which are new and lack precise information about function or molecular mechanism. Here we present a fast method to predict potential phosphorylation switches by mapping phosphorylation sites...

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Bibliographische Detailangaben
Hauptverfasser: Betts, Matthew J. (VerfasserIn) , Wichmann, Oliver (VerfasserIn) , Utz, Mathias (VerfasserIn) , André, Timon (VerfasserIn) , Gavin, Anne-Claude (VerfasserIn) , Bork, Peer (VerfasserIn) , Russell, Robert B. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2017
In: PLoS Computational Biology
Year: 2017, Jahrgang: 13, Heft: 3
ISSN:1553-7358
DOI:10.1371/journal.pcbi.1005462
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1371/journal.pcbi.1005462
Verlag, kostenfrei, Volltext: http://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1005462
Volltext
Verfasserangaben:Matthew J. Betts, Oliver Wichmann, Mathias Utz, Timon Andre, Evangelia Petsalaki, Pablo Minguez, Luca Parca, Frederick P. Roth, Anne-Claude Gavin, Peer Bork, Robert B. Russell
Beschreibung
Zusammenfassung:Proteomics techniques can identify thousands of phosphorylation sites in a single experiment, the majority of which are new and lack precise information about function or molecular mechanism. Here we present a fast method to predict potential phosphorylation switches by mapping phosphorylation sites to protein-protein interactions of known structure and analysing the properties of the protein interface. We predict 1024 sites that could potentially enable or disable particular interactions. We tested a selection of these switches and showed that phosphomimetic mutations indeed affect interactions. We estimate that there are likely thousands of phosphorylation mediated switches yet to be uncovered, even among existing phosphorylation datasets. The results suggest that phosphorylation sites on globular, as distinct from disordered, parts of the proteome frequently function as switches, which might be one of the ancient roles for kinase phosphorylation.
Beschreibung:Published: March 27, 2017
Gesehen am 12.06.2018
Beschreibung:Online Resource
ISSN:1553-7358
DOI:10.1371/journal.pcbi.1005462

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