Evidence map›Paper›PMID 8920860›Full record

ArticleThe Journal of experimental medicine1996

Characterization of Cbl tyrosine phosphorylation and a Cbl-Syk complex in RBL-2H3 cells.

Y Ota, L O Beitz, A M Scharenberg, J A Donovan, J P Kinet, L E Samelson

Abstract read
In one paragraph

Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
  4. C-Cbl negatively regulates TRAF6-mediated NF-Cellular & molecular biology letters · 2019
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Lipid rafts in mast cell biology.Journal of lipids · 2011
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Kinase activation through dimerization by human SH2-B.Molecular and cellular biology · 2005
    Article
  16. Article
  17. Review
  18. Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling.Proceedings of the National Academy of Sciences of the United States of America · 2001
    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

6 authors.

Y OtaCell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, Maryland 20892-5430, USA.
L O Beitz
A M Scharenberg
J A Donovan
J P Kinet
L E Samelson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine phosphorylation of the Cbl protooncogene has been shown to occur after engagement of a number of different receptors on hematopoietic cells. However, the mechanisms by which these receptors induce Cbl tyrosine phosphorylation are poorly understood. Here we demonstrate that engagement of the high affinity IgE receptor (Fc epsilon R1) leads to the tyrosine phosphorylation of Cbl and analyze how this occurs. We show that at least part of Fc epsilon R1-induced Cbl tyrosine phosphorylation is mediated by the Syk tyrosine kinase, and that the Syk-dependent tyrosine phosphorylation of Cbl occurs mainly distal to the Cbl proline-rich region within the COOH-terminal 250 amino acids. Furthermore, we show by coprecipitation that Cbl is present in a complex with Syk before receptor engagement, that the proline-rich region of Cbl and a region of Syk comprised of the two SH2 domains and intradomain linker are required for formation of the complex, and that little or no tyrosine-phosphorylated Cbl is detected in complex with Syk. Overexpression of truncation mutants of Cbl capable of binding Syk has the effect of blocking tyrosine phosphorylation of endogenous Cbl. These results define a potentially important intramolecular interaction in mast cells and suggest a complex function for Cbl in intracellular signaling pathways.

Indexed as

Ubiquitin-Protein LigasesAnimalsCell LineDNA Mutational AnalysisEnzyme ActivationEnzyme PrecursorsIntracellular Signaling Peptides and ProteinsMast CellsMiceMutationPhosphorylationProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-cblRatsCBL protein, humanCbl protein, mouseEnzyme PrecursorsIntracellular Signaling Peptides and ProteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-cblReceptors, IgERecombinant Proteinssrc-Family KinasesSyk KinaseSYK protein, humanSyk protein, mouseSyk protein, ratTyrosineUbiquitin-Protein Ligases

Identifiers

PMID8920860
PMCPMC2192902

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Registered trials

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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.