Evidence map›Paper›PMID 10391677›Full record

ArticleOncogene1999

SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis.

L Rönnstrand, A K Arvidsson, A Kallin, C Rorsman, U Hellman, U Engström, C Wernstedt, C H Heldin

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.6field-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

31 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

L RönnstrandLudwig Institute for Cancer Research, Biomedical Centre, Uppsala, Sweden.
A K Arvidsson
A Kallin
C Rorsman
U Hellman
U Engström
C Wernstedt
C H Heldin
Ludwig Cancer Research · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the beta-receptor for platelet-derived growth factor (PDGF) by its ligand leads to autophosphorylation on a number of tyrosine residues. Here we show that Tyr763 in the kinase insert region is a novel autophosphorylation site, which after phosphorylation binds the protein tyrosine phosphatase SHP-2. SHP-2 has also previously been shown to bind to phosphorylated Tyr1009 in the PDGF beta-receptor. Porcine aortic endothelial (PAE) cells transfected with a PDGF beta-receptor in which Tyr763 and Tyr1009 were mutated to phenylalanine residues failed to associate with SHP-2 after ligand stimulation. Moreover, PDGF-BB-induced Ras GTP-loading and Erk2 activation were severely compromised in the receptor mutant. Whereas the mitogenic response to PDGF-BB remained at the same level as in cells expressing wild-type PDGF beta-receptor, chemotaxis induced by PDGF-BB was significantly decreased in the case of the Y763F/Y1009F mutant cells, suggesting an important role for SHP-2 in chemotactic signaling.

Indexed as

ChemotaxisProtein Processing, Post-TranslationalSignal TransductionAmino Acid SequenceAnimalsBecaplerminBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCells, CulturedEndothelium, VascularEnzyme ActivationGuanosine TriphosphateIntracellular Signaling Peptides and ProteinsMiceMitogen-Activated Protein Kinase 1Molecular Sequence DataBecaplerminCalcium-Calmodulin-Dependent Protein KinasesGuanosine TriphosphateIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein Kinase 1PhosphotyrosinePlatelet-Derived Growth FactorProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProto-Oncogene Proteins c-sisPtpn11 protein, mousePtpn6 protein, mouseras ProteinsReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorTyrosine

Identifiers

PMID10391677
OpenAlexW1975735851

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.