Evidence map›Paper›PMID 30228194›Full record

ArticleMolecular & cellular proteomics : MCP2018

A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans.

Scott P Lyons, Nicole P Jenkins, Isha Nasa, Meng S Choy, Mark E Adamo, Rebecca Page, Wolfgang Peti, Greg B Moorhead, Arminja N Kettenbach

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

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  5. A protein phosphatase 1 specificProceedings of the National Academy of Sciences of the United States of America · 2024
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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

9 authors at 4 institutions in 2 countries.

Scott P LyonsDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, USA.
Nicole P JenkinsNorris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center at Dartmouth, Lebanon, NH, USA.
Isha NasaDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, USA; Norris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center at Dartmouth, Lebanon, NH, USA.
Meng S ChoyDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Mark E AdamoNorris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center at Dartmouth, Lebanon, NH, USA.
Rebecca PageDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Wolfgang PetiDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Greg B MoorheadDepartment of Biological Science, University of Calgary, Alberta, Canada.
Arminja N KettenbachDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, USA; Norris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center at Dartmouth, Lebanon, NH, USA. Electronic address: Arminja.N.Kettenbach@dartmouth.edu.
Dartmouth College · USUniversity of Arizona · USDartmouth–Hitchcock Medical Center · USUniversity of Calgary · CA

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
Phosphorylation Signaling by Phosphoprotein PhosphatasesR35GM119455 · NIGMS · DARTMOUTH COLLEGE · PI Arminja Nadine Kettenbach · 2016 to 2026
$5.1M
LC-Orbitrap MS/MS System for shotgun Proteomics at DartmouthS10OD016212 · OD · DARTMOUTH COLLEGE · PI GERBER, SCOTT A. · 2013 to 2013
$600k
NCI NIH HHS P30 CA023108NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R35 GM119455NIH HHS S10 OD016212
6 · The paper itself

Abstract

A "tug-of-war" between kinases and phosphatases establishes the phosphorylation states of proteins. While serine and threonine phosphorylation can be catalyzed by more than 400 protein kinases, the majority of serine and threonine dephosphorylation is carried out by seven phosphoprotein phosphatases (PPPs). The PPP family consists of protein phosphatases 1 (PP1), 2A (PP2A), 2B (PP2B), 4 (PP4), 5 (PP5), 6 (PP6), and 7 (PP7). The imbalance in numbers between serine- and threonine-directed kinases and phosphatases led to the early belief that PPPs are unspecific and that kinases are the primary determinants of protein phosphorylation. However, it is now clear that PPPs achieve specificity through association with noncatalytic subunits to form multimeric holoenzymes, which expands the number of functionally distinct signaling entities to several hundred. Although there has been great progress in deciphering signaling by kinases, much less is known about phosphatases.We have developed a chemical proteomic strategy for the systematic interrogation of endogenous PPP catalytic subunits and their interacting proteins, including regulatory and scaffolding subunits (the "PPPome"). PP1, PP2A, PP4, PP5, and PP6 were captured using an immobilized, specific but nonselective PPP inhibitor microcystin-LR (MCLR), followed by protein identification by liquid chromatography-tandem mass spectrometry (LC-MS/MS) in a single analysis. Here, we combine this approach of phosphatase inhibitor bead profiling and mass spectrometry (PIB-MS) with label-free and tandem mass tag (TMT) quantification to map the PPPome in human cancer cell lines, mouse tissues, and yeast species, through which we identify cell- and tissue-type-specific PPP expression patterns and discover new PPP interacting proteins.

Indexed as

Catalytic DomainAnimalsChromatography, LiquidHeLa CellsHumansMarine ToxinsMCF-7 CellsMiceMicrocystinsNeoplasmsPhosphoprotein PhosphatasesPhosphorylationProtein BindingProteomicsSaccharomyces cerevisiaeSignal Transductioncyanoginosin LRMarine ToxinsMicrocystinsPhosphoprotein PhosphatasesAffinity proteomicsPhosphorylationProtein complex analysisProtein PhosphatasesProtein-Protein InteractionsQuantification

Identifiers

PMID30228194
PMCPMC6283287
OpenAlexW2890662474

What OpenQuestion holds

Textmetadata
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.