Evidence map›Paper›PMID 21551504›Full record

ArticleMolecular & cellular proteomics : MCP2011

Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes.

Ronghu Wu, Noah Dephoure, Wilhelm Haas, Edward L Huttlin, Bo Zhai, Mathew E Sowa, Steven P Gygi

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 1 pooled it
6.8field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 1 synthesis or guideline pooled it, 190 citations in OpenAlex.

  1. Pooled it
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  5. Review
  6. Review
  7. In-Depth Analysis of Tissue Phosphoproteomics with TiOMethods in molecular biology (Clifton, N.J.) · 2025
    Article
  8. Review
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41 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Ronghu WuDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Noah Dephoure
Wilhelm Haas
Edward L Huttlin
Bo Zhai
Mathew E Sowa
Steven P Gygi
Harvard University · US

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
New Technologies for Quantitative Phosphorylation AnalysisR01HG003456 · NHGRI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2005 to 2011
$2.7M
NHGRI NIH HHS HG3456NHGRI NIH HHS R01 HG003456NIGMS NIH HHS GM67945NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

The interpretation of quantitative phosphoproteomics studies is complicated because each differential phosphorylation event integrates both changes in protein expression and phosphorylation. Here we investigated this phenomenon by performing parallel comparisons of protein expression and phosphorylation in S. cerevisiae. In each of two experiments comparing yeast mutants bearing deletions in FUS3 or STE7 with their wild-type counterparts, we quantified over 4100 proteins, including all members of the yeast mating pathway. We also identified 12,499 unique phosphorylation sites in this work. We demonstrate the critical importance of controlling the protein-level false-discovery rate and provide a novel method to assess the accuracy of protein false-discovery rate estimates. For the first time, 96% of nonredundant phosphopeptide ratios could be calibrated by protein levels, allowing truly differential phosphorylation to be distinguished from altered protein expression. This revealed a starkly different view, with 25% of seemingly differential phosphopeptides now attributed to changes in protein expression. Combined protein expression and phosphorylation surveys uncovered both independent and concerted changes in protein expression and phosphorylation, while highlighting the partially redundant role of a second MAPK (Kss1) in the mating pathway.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCalibrationGene ExpressionGene Knockout TechniquesMAP Kinase Signaling SystemMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPhosphoproteinsPhosphorylationProtein KinasesProteomeReproduction, AsexualSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFUS3 protein, S cerevisiaeKSS1 protein, S cerevisiaeMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPhosphoproteinsProtein KinasesProteomeSaccharomyces cerevisiae ProteinsSTE7 protein, S cerevisiae

Identifiers

PMID21551504
PMCPMC3149096
OpenAlexW2038801176

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.