Evidence map›Paper›PMID 20489023›Full record

ArticleScience (New York, N.Y.)2010

A global protein kinase and phosphatase interaction network in yeast.

Ashton Breitkreutz, Hyungwon Choi, Jeffrey R Sharom, Lorrie Boucher, Victor Neduva, Brett Larsen, Zhen-Yuan Lin, Bobby-Joe Breitkreutz, Chris Stark, Guomin Liu and 10 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 380 papers.

0numbers the graph read from it
0cells of the map it votes in
380citing papers in PubMed
36.4field-weighted citation impact, top 1% 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

380 citing papers in PubMed, 693 citations in OpenAlex.

  1. Article
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  9. NAR genomics and bioinformatics · 2026
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  15. Article
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  17. Integrative Phosphoproteomic and Proteomic Analysis ofJournal of proteome research · 2025
    Article
  18. Article
  19. Article
  20. Article

320 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 1 institution in 1 country.

Ashton BreitkreutzCentre for Systems Biology, Samuel Lunenfeld Research Institute, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada.
Hyungwon Choi
Jeffrey R Sharom
Lorrie Boucher
Victor Neduva
Brett Larsen
Zhen-Yuan Lin
Bobby-Joe Breitkreutz
Chris Stark
Guomin Liu
Jessica Ahn
Danielle Dewar-Darch
Teresa Reguly
Xiaojing Tang
Ricardo Almeida
Zhaohui Steve Qin
Tony Pawson
Anne-Claude Gingras
Alexey I Nesvizhskii
Mike Tyers
University of Michigan–Ann Arbor · US

Funding

BioGRID: An open resource for biological interactions and network analysisR01OD010929 · OD · SINAI HEALTH SYSTEM · PI KARA DOLINSKI, Mike Tyers · 2012 to 2026
$13.9M
COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
BioGRID: an open resource for biological interactions and network analysisR01RR024031 · NCRR · SINAI HEALTH SYSTEM · PI TYERS, MIKE · 2007 to 2011
$3.2M
Analysis and Statistical Validation of Proteomic DatasetsR01CA126239 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NESVIZHSKII, ALEXEY I · 2006 to 2009
$1.2M
CIHR MOP-12246CIHR MOP-57793CIHR MOP-84314NCI NIH HHS CA-126239NCI NIH HHS R01 CA126239NCRR NIH HHS R01 RR024031NCRR NIH HHS R01RR024031NIGMS NIH HHS R01 GM094231NIH HHS R01 OD010929
6 · The paper itself

Abstract

The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with multiple kinases that revealed roles for Cdc14 in mitogen-activated protein kinase signaling, the DNA damage response, and metabolism, whereas interactions of the target of rapamycin complex 1 (TORC1) uncovered new effector kinases in nitrogen and carbon metabolism. An extensive backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.

Indexed as

Binding SitesCarbonCell Cycle ProteinsDNA DamageMAP Kinase Signaling SystemMass SpectrometryMetabolic Networks and PathwaysModels, BiologicalNitrogenPhosphoprotein PhosphatasesPhosphorylationProtein Interaction MappingProtein KinasesProtein Serine-Threonine KinasesProtein SubunitsProtein Tyrosine PhosphatasesCarbonCDC14 protein, S cerevisiaeCell Cycle ProteinsNitrogenPhosphoprotein PhosphatasesProtein KinasesProtein Serine-Threonine KinasesProtein SubunitsProtein Tyrosine PhosphatasesProteomeSaccharomyces cerevisiae Proteinstarget of rapamycin protein, S cerevisiae

Identifiers

PMID20489023
PMCPMC3983991
OpenAlexW2157421521

What OpenQuestion holds

Textmetadata
LicenceTDM
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.