Evidence map›Paper›PMID 26503604›Full record

ArticleJournal of proteome research2015

Multiplexed, Proteome-Wide Protein Expression Profiling: Yeast Deubiquitylating Enzyme Knockout Strains.

Marta Isasa, Christopher M Rose, Suzanne Elsasser, José Navarrete-Perea, Joao A Paulo, Daniel J Finley, Steven P Gygi

Abstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 62 citations in OpenAlex.

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  10. Blistering1 ModulatesMolecular & cellular proteomics : MCP · 2020
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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

7 authors at 2 institutions in 2 countries.

Marta IsasaDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Christopher M RoseDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Suzanne ElsasserDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
José Navarrete-PereaNational Autonomous University of Mexico, Av. Universidad 3000, Mexico City, District Federal 04510, Mexico.
Joao A PauloDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Daniel J FinleyDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Steven P GygiDepartment of Cell Biology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Harvard University · USUniversidad Nacional Autónoma de México · MX

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Resolving the role of nicotine-mediated phosphorylation on pancreatic fibrosisK01DK098285 · NIDDK · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2013 to 2017
$638k
NIDDK NIH HHS K01 DK098285NIGMS NIH HHS GM67945NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

Characterizing a protein's function often requires a description of the cellular state in its absence. Multiplexing in mass spectrometry-based proteomics has now achieved the ability to globally measure protein expression levels in yeast from 10 cell states simultaneously. We applied this approach to quantify expression differences in wild type and nine deubiquitylating enzyme (DUB) knockout strains with the goal of creating "information networks" that might provide deeper, mechanistic insights into a protein's biological role. In total, more than 3700 proteins were quantified with high reproducibility across three biological replicates (30 samples in all). DUB mutants demonstrated different proteomics profiles, consistent with distinct roles for each family member. These included differences in total ubiquitin levels and specific chain linkages. Moreover, specific expression changes suggested novel functions for several DUB family members. For instance, the ubp3Δ mutant showed large expression changes for members of the cytochrome C oxidase complex, consistent with a role for Ubp3 in mitochondrial regulation. Several DUBs also showed broad expression changes for phosphate transporters as well as other components of the inorganic phosphate signaling pathway, suggesting a role for these DUBs in regulating phosphate metabolism. These data highlight the potential of multiplexed proteome-wide analyses for biological investigation and provide a framework for further study of the DUB family. Our methods are readily applicable to the entire collection of yeast deletion mutants and may help facilitate systematic analysis of yeast and other organisms.

Indexed as

Electron Transport Complex IVEndopeptidasesGene DeletionGene Knockout TechniquesGenes, FungalNuclear ProteinsPhosphatesProtein Array AnalysisProteomeProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionUbiquitinUbiquitin-Specific ProteasesUbiquitin ThiolesteraseElectron Transport Complex IVEndopeptidasesNuclear ProteinsOtu1 protein, S cerevisiaePhosphatesProteomeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUBP10 protein, S cerevisiaeUbp15 protein, S cerevisiaeUBP3 protein, S cerevisiaeCOX complexdeubiquitinaseshigh-throughput proteomicsinorganic phosphate pathwayisobaric labelingOrbitrap Fusionquantitative proteomicsTMTubiquitinUBP3

Identifiers

PMID26503604
PMCPMC4802358
OpenAlexW2238015745

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.