Evidence map›Paper›PMID 29514104›Full record

ArticleCell reports2018

Large-Scale Phosphoproteomics Reveals Shp-2 Phosphatase-Dependent Regulators of Pdgf Receptor Signaling.

Tanveer S Batth, Moreno Papetti, Anamarija Pfeiffer, Maxim A X Tollenaere, Chiara Francavilla, Jesper V Olsen

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Complex Roles ofAnnual review of cancer biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. A comprehensive review of SHP2 and its role in cancer.Cellular oncology (Dordrecht, Netherlands) · 2022
    Review
  17. Review
  18. Article
  19. Article
  20. Targeting SHP2 phosphatase in hematological malignancies.Expert opinion on therapeutic targets · 2022
    Review
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

6 authors at 2 institutions in 2 countries.

Tanveer S BatthProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Science, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Moreno PapettiProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Science, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Anamarija PfeifferProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Science, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Maxim A X TollenaereCellular Stress Signaling Group, Department of Cellular and Molecular Medicine, Center for Healthy Aging, University of Copenhagen, 2200 Copenhagen, Denmark.
Chiara FrancavillaProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Science, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark; School of Biological Sciences, FBMH, University of Manchester, Oxford Road, Manchester M13 9PT, UK. Electronic address: chiara.francavilla@manchester.ac.uk.
Jesper V OlsenProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Science, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark. Electronic address: jesper.olsen@cpr.ku.dk.
Novo Nordisk Foundation · DKUniversity of Copenhagen · DK

Funding

Wellcome Trust 107636Wellcome Trust 8107636/Z/15/Z
6 · The paper itself

Abstract

Despite its low cellular abundance, phosphotyrosine (pTyr) regulates numerous cell signaling pathways in health and disease. We applied comprehensive phosphoproteomics to unravel differential regulators of receptor tyrosine kinase (RTK)-initiated signaling networks upon activation by Pdgf-ββ, Fgf-2, or Igf-1 and identified more than 40,000 phosphorylation sites, including many phosphotyrosine sites without additional enrichment. The analysis revealed RTK-specific regulation of hundreds of pTyr sites on key signaling molecules. We found the tyrosine phosphatase Shp-2 to be the master regulator of Pdgfr pTyr signaling. Application of a recently introduced allosteric Shp-2 inhibitor revealed global regulation of the Pdgf-dependent tyrosine phosphoproteome, which significantly impaired cell migration. In addition, we present a list of hundreds of Shp-2-dependent targets and putative substrates, including Rasa1 and Cortactin with increased pTyr and Gab1 and Erk1/2 with decreased pTyr. Our study demonstrates that large-scale quantitative phosphoproteomics can precisely dissect tightly regulated kinase-phosphatase signaling networks.

Indexed as

ProteomicsSignal TransductionAnimalsAntibodiesBecaplerminEnzyme ActivationFocal Adhesion Protein-Tyrosine KinasesLigandsMiceNIH 3T3 CellsPhosphoproteinsPhosphorylationPhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 11ProteomeReceptors, Platelet-Derived Growth FactorAntibodiesBecaplerminFocal Adhesion Protein-Tyrosine KinasesLigandsPhosphoproteinsPhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 11ProteomeReceptors, Platelet-Derived Growth Factorlabel-free quantitationmass spectrometryorbitrapPDGFphosphoproteomicsQ exactiveSHP099Shp-2TiO2tyrosine phosphorylation

Identifiers

PMID29514104
PMCPMC7618100
OpenAlexW2792103163

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.