Evidence map›Paper›PMID 8440263›Full record

ArticleThe EMBO journal1993

Association of p56lck with IL-2 receptor beta chain is critical for the IL-2-induced activation of p56lck.

Y Minami, T Kono, K Yamada, N Kobayashi, A Kawahara, R M Perlmutter, T Taniguchi

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Signal-transduction defects in T cells.Clinical reviews in allergy & immunology · 2001
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  15. Article
  16. Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  17. Evolution of the src-related protein tyrosine kinases.Journal of molecular evolution · 1996
    Article
  18. Article
  19. Involvement of p59fynT in interleukin-5 receptor signaling.The Journal of experimental medicine · 1995
    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

7 authors at 1 institution in 1 country.

Y MinamiInstitute for Molecular and Cellular Biology, Osaka University, Japan.
T Kono
K Yamada
N Kobayashi
A Kawahara
R M Perlmutter
T Taniguchi
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies demonstrate that p56lck, a member of the src-family of protein tyrosine kinases (PTKs), can physically associate with the interleukin-2 (IL-2) receptor beta chain (IL-2R beta) and that IL-2 receptor engagement stimulates p56lck activity. To examine the mechanisms underlying p56lck PTK activation by IL-2, we established a mouse pro-B cell line, BAF-B03, expressing both IL-2R beta (either the wild-type or mutant forms) and mouse p56lck at high levels. BAF-B03 cells expressing a mutant IL-2R beta chain lacking an 'acidic' region of the cytoplasmic domain, previously shown to be essential for association with p56lck, fail to induce p56lck PTK activation upon IL-2 stimulation. This suggests that the association of p56lck with the IL-2R beta chain, despite its low stoichiometry, is required for the activation of cellular p56lck PTK upon IL-2 stimulation. Intriguingly, BAF-B03 cells expressing an IL-2R beta chain which lacks a different cytoplasmic region, the 'serine-rich' region, also fail to activate p56lck in response to IL-2. Hence, physical association of p56lck with the IL-2R beta chain is not by itself sufficient to permit IL-2-mediated regulation of this PTK. Additional experiments suggest that one result of PTK activation is the accumulation of c-fos and c-jun transcripts.

Indexed as

AnimalsB-LymphocytesCells, CulturedEnzyme ActivationGene ExpressionGenes, fosGenes, junHumansInterleukin-2Lymphocyte Specific Protein Tyrosine Kinase p56(lck)MiceMutationProtein-Tyrosine KinasesReceptors, Interleukin-2Signal TransductionInterleukin-2Lymphocyte Specific Protein Tyrosine Kinase p56(lck)Protein-Tyrosine KinasesReceptors, Interleukin-2

Identifiers

PMID8440263
PMCPMC413263
OpenAlexW2202198491

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.