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Conserved phosphorylation hotspots in eukaryotic protein domain families

Marta J. Strumillo, Michaela Oplová, Cristina Viéitez, David Ochoa, Mohammed Shahraz, Bede P. Busby, Richelle Sopko, Romain A. Studer, Norbert Perrimon, Vikram G. Panse, Pedro Beltrao
doi: https://doi.org/10.1101/391185
Marta J. Strumillo
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
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Michaela Oplová
2Institute of Medical Microbiology, University of Zurich, CH-8006 Zurich, Switzerland;
3Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland
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Cristina Viéitez
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
4European Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany
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David Ochoa
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
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Mohammed Shahraz
4European Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany
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Bede P. Busby
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
4European Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany
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Richelle Sopko
5Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115
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Romain A. Studer
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
6Corrent address: BenevolentAI, London NW1 1LW, UK.
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Norbert Perrimon
5Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115
7Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115
8Howard Hughes Medical Institute, 77 Avenue Louis Pasteur, Boston, MA 02115
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Vikram G. Panse
2Institute of Medical Microbiology, University of Zurich, CH-8006 Zurich, Switzerland;
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Pedro Beltrao
1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, CB10 1SD, Cambridge, UK
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  • For correspondence: pbeltrao@ebi.ac.uk
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Abstract

Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. While the inventory for phosphorylation sites across different species has rapidly expanded, their functional role remains poorly investigated. Here, we have combined 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation “hotspot” regions within domain families. Mapping these regions onto structural data revealed that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Notably, functional studies of a phospho-deficient mutant in the C-terminal hotspot region within the Ribosomal S11 domain in the yeast ribosomal protein uS11 showed cold-sensitive phenotype and impaired 20S pre-rRNA processing. Altogether, our study identified phosphorylation hotspots for 162 protein domains suggestive of an ancient role for the control of diverse eukaryotic domain families.

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Posted August 13, 2018.
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Conserved phosphorylation hotspots in eukaryotic protein domain families
Marta J. Strumillo, Michaela Oplová, Cristina Viéitez, David Ochoa, Mohammed Shahraz, Bede P. Busby, Richelle Sopko, Romain A. Studer, Norbert Perrimon, Vikram G. Panse, Pedro Beltrao
bioRxiv 391185; doi: https://doi.org/10.1101/391185
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Conserved phosphorylation hotspots in eukaryotic protein domain families
Marta J. Strumillo, Michaela Oplová, Cristina Viéitez, David Ochoa, Mohammed Shahraz, Bede P. Busby, Richelle Sopko, Romain A. Studer, Norbert Perrimon, Vikram G. Panse, Pedro Beltrao
bioRxiv 391185; doi: https://doi.org/10.1101/391185

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