Evidence map›Paper›PMID 28346509›Full record

ArticlePLoS computational biology2017

Systematic identification of phosphorylation-mediated protein interaction switches.

Matthew J Betts, Oliver Wichmann, Mathias Utz, Timon Andre, Evangelia Petsalaki, Pablo Minguez, Luca Parca, Frederick P Roth, Anne-Claude Gavin, Peer Bork and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 57 citations in OpenAlex.

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  9. Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024
    Review
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  11. Article
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  14. Towards a structurally resolved human protein interaction network.Nature structural & molecular biology · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 3 countries.

Matthew J BettsCellNetworks, Bioquant, University of Heidelberg, Im Neuenheimer Feld 267, Heidelberg, Germany.ORCID 0000-0003-4583-9814
Oliver WichmannCellNetworks, Bioquant, University of Heidelberg, Im Neuenheimer Feld 267, Heidelberg, Germany.
Mathias UtzCellNetworks, Bioquant, University of Heidelberg, Im Neuenheimer Feld 267, Heidelberg, Germany.
Timon AndreCellNetworks, Bioquant, University of Heidelberg, Im Neuenheimer Feld 267, Heidelberg, Germany.
Evangelia PetsalakiLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, Canada.ORCID 0000-0002-8294-2995
Pablo MinguezEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany.
Luca ParcaEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany.
Frederick P RothLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, Canada.
Anne-Claude GavinEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany.
Peer BorkEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, Germany.
Robert B RussellCellNetworks, Bioquant, University of Heidelberg, Im Neuenheimer Feld 267, Heidelberg, Germany.
Heidelberg University · DEEuropean Molecular Biology Laboratory · DECanadian Institute for Advanced Research · CAMount Sinai Hospital · CA

Funding

Genomic Analysis of Network Perturbations in Human DiseaseP50HG004233 · NHGRI · DANA-FARBER CANCER INST · PI VIDAL, MARC · 2007 to 2017
$31.6M
Resource ProjectU41HG001715 · NHGRI · DANA-FARBER CANCER INST · PI HILL, DAVID E. · 2015 to 2017
$4.7M
NHGRI NIH HHS P50 HG004233NHGRI NIH HHS U41 HG001715
6 · The paper itself

Abstract

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.

Indexed as

Models, ChemicalBinding SitesComputer SimulationModels, MolecularPhosphorylationPhosphotransferasesProtein BindingProtein ConformationProtein Interaction MappingProteomeSequence Analysis, ProteinStructure-Activity RelationshipPhosphotransferasesProteome

Identifiers

PMID28346509
PMCPMC5386296
OpenAlexW2599616891

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.