Evidence map›Paper›PMID 18948260›Full record

ArticleThe Journal of biological chemistry2008

Activation of c-Src and Fyn kinases by protein-tyrosine phosphatase RPTPalpha is substrate-specific and compatible with lipid raft localization.

Nathalie Vacaresse, Bente Møller, E Michael Danielsen, Masato Okada, Jan Sap

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Protein tyrosine phosphatase α in the dorsomedial striatum promotes excessive ethanol-drinking behaviors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  15. Loss of branched O-mannosyl glycans in astrocytes accelerates remyelination.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    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

5 authors at 4 institutions in 3 countries.

Nathalie VacaresseBiotech Research and Innovation Center, Copenhagen Biocenter, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark.
Bente Møller
E Michael Danielsen
Masato Okada
Jan Sap
New York University · USBioInnovation Institute · DKOsaka University · JPUniversity of Copenhagen · DK

Funding

Study of Receptor Protein Tyrosine Phosphatase AlphaR01CA087005 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SAP, JAN M · 2001 to 2005
$1.2M
NCI NIH HHS R01 CA87005
6 · The paper itself

Abstract

Src family tyrosine kinases (SFKs) function in multiple signaling pathways, raising the question of how appropriate regulation and substrate choice are achieved. SFK activity is modulated by several protein-tyrosine phosphatases, among which RPTPalpha and SHP2 are the best established. We studied how RPTPalpha affects substrate specificity and regulation of c-Src and Fyn in response to epidermal growth factor and platelet-derived growth factor. We find that RPTPalpha, in a growth factor-specific manner, directs the specificity of these kinases toward a specific subset of SFK substrates, particularly the focal adhesion protein Paxillin and the lipid raft scaffolding protein Cbp/PAG. A significant fraction of RPTPalpha is present in lipid rafts, where its targets Fyn and Cbp/PAG reside, and growth factor-mediated SFK activation within this compartment is strictly dependent on RPTPalpha. Forced concentration of RPTPalpha into lipid rafts is compatible with activation of Fyn. Finally, RPTPalpha-induced phosphorylation of Paxillin and Cbp/PAG induces recruitment of the SFK inhibitory kinase Csk, indicative of negative feedback loops limiting SFK activation by RPTPalpha. Our findings indicate that individual SFK-controlling PTPs play important and specific roles in dictating SFK substrate specificity and regulatory mechanism.

Indexed as

AnimalsCell LineEnzyme ActivationEpidermal Growth FactorGenes, srcIntercellular Signaling Peptides and ProteinsMembrane MicrodomainsMembrane ProteinsMiceMice, KnockoutPaxillinPhosphoproteinsPlatelet-Derived Growth FactorProtein Tyrosine Phosphatase, Non-Receptor Type 11Proto-Oncogene Proteins c-fynReceptor-Like Protein Tyrosine Phosphatases, Class 4Epidermal Growth FactorFyn protein, mouseIntercellular Signaling Peptides and ProteinsMembrane ProteinsPag protein, mousePaxillinPhosphoproteinsPlatelet-Derived Growth FactorProtein Tyrosine Phosphatase, Non-Receptor Type 11Proto-Oncogene Proteins c-fynPtpn11 protein, mousePtpra protein, mousePxn protein, mouseReceptor-Like Protein Tyrosine Phosphatases, Class 4

Identifiers

PMID18948260
PMCPMC2602903
OpenAlexW1976119455

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.