Evidence map›Paper›PMID 20071362›Full record

ArticleMolecular & cellular proteomics : MCP2010

An integrated phosphoproteomics work flow reveals extensive network regulation in early lysophosphatidic acid signaling.

Thiemo B Schreiber, Nina Mäusbacher, György Kéri, Jürgen Cox, Henrik Daub

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Regulation of the microprocessor by post-translational modifications.Frontiers in cell and developmental biology · 2025
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  5. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond.Journal of molecular and cellular cardiology · 2014
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR).Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
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

5 authors at 2 institutions in 2 countries.

Thiemo B SchreiberCell Signaling Group, Department of Molecular Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Nina Mäusbacher
György Kéri
Jürgen Cox
Henrik Daub
Max Planck Institute of Biochemistry · DESemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysophosphatidic acid (LPA) induces a variety of cellular signaling pathways through the activation of its cognate G protein-coupled receptors. To investigate early LPA responses and assess the contribution of epidermal growth factor (EGF) receptor transactivation in LPA signaling, we performed phosphoproteomics analyses of both total cell lysate and protein kinase-enriched fractions as complementary strategies to monitor phosphorylation changes in A498 kidney carcinoma cells. Our integrated work flow enabled the identification and quantification of more than 5,300 phosphorylation sites of which 224 were consistently regulated by LPA. In addition to induced phosphorylation events, we also obtained evidence for early dephosphorylation reactions due to rapid phosphatase regulation upon LPA treatment. Phosphorylation changes induced by direct heparin-binding EGF-like growth factor-mediated EGF receptor activation were typically weaker and only detected on a subset of LPA-regulated sites, indicating signal integration among EGF receptor transactivation and other LPA-triggered pathways. Our results reveal rapid phosphoregulation of many proteins not yet implicated in G protein-coupled receptor signaling and point to various additional mechanisms by which LPA might regulate cell survival and migration as well as gene transcription on the molecular level. Moreover, our phosphoproteomics analysis of both total lysate and kinase-enriched fractions provided highly complementary parts of the LPA-regulated signaling network and thus represents a useful and generic strategy toward comprehensive signaling studies on a system-wide level.

Indexed as

Signal TransductionCell ExtractsCell Line, TumorComputational BiologyEnzyme ActivationHeparin-binding EGF-like Growth FactorHumansIntercellular Signaling Peptides and ProteinsIsotope LabelingLysophospholipidsMass SpectrometryPhosphoproteinsPhosphorylationProtein KinasesProteomicsReproducibility of ResultsCell ExtractsHBEGF protein, humanHeparin-binding EGF-like Growth FactorIntercellular Signaling Peptides and Proteinslysophosphatidic acidLysophospholipidsPhosphoproteinsProtein Kinases

Identifiers

PMID20071362
PMCPMC2877970
OpenAlexW2005325127

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.