Evidence map›Paper›PMID 8887542›Full record

ArticleThe EMBO journal1996

Interleukin-4-specific signal transduction events are driven by homotypic interactions of the interleukin-4 receptor alpha subunit.

S Y Lai, J Molden, K D Liu, J M Puck, M D White, M A Goldsmith

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

10 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Interaction affinity between cytokine receptor components on the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  5. Targeted disruption of the interferon-gamma receptor 2 gene results in severe immune defects in mice.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  6. Article
  7. Review
  8. Receptor-associated constitutive protein tyrosine phosphatase activity controls the kinase function of JAK1.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  9. Article
  10. 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 at 2 institutions in 1 country.

S Y LaiGladstone Institute of Virology and Immunology, University of California, San Francisco, USA.
J Molden
K D Liu
J M Puck
M D White
M A Goldsmith
Gladstone Institutes · USUniversity of California, San Francisco · US

Funding

Signal Transduction by Cytokine Receptors in VivoR01GM054351 · NIGMS · J. DAVID GLADSTONE INSTITUTES · PI GREENE, WARNER C · 1995 to 2004
$1.3M
NIGMS NIH HHS GM54351-01
6 · The paper itself

Abstract

Interleukin-4 (IL-4) exerts its effects through a heterodimeric receptor complex (IL-4R), which contains the IL-4R(alpha) and gamma(c) subunits. IL-4R(alpha) also functions with other partner subunits in several receptor types, including the IL-13 receptor. To examine the roles of the individual subunits within IL-4R complexes, we employed a chimeric system that recapitulates native IL-4R function as verified by the activation of the kinases, JAK1 and JAK3, and induction of STAT-6. When a mutant gamma(c) subunit in which the four cytoplasmic tyrosines were converted to phenylalanine was paired with the cytoplasmic domain of the IL-4R(alpha) chain, specificity within the JAK-STAT pathway was not altered. Signaling events were examined further in cells expressing the IL-4R(alpha) chimera alone without the gamma(c) chimera. Ligand-induced homodimerization of these receptors activated the IL-4 signaling program despite the absence of gamma(c), including induction of JAK1 and STAT-6, phosphorylation of the insulin-related substrate 1 and cellular proliferation. Thus, homotypic interactions of the IL-4R(alpha) subunit are sufficient for the initiation and determination of IL-4-specific signaling events, and such interactions may be integral to signaling through IL-4R complexes.

Indexed as

Signal TransductionAnimalsAntigens, CDCell LineEnzyme ActivationInsulin Receptor Substrate ProteinsInterleukin-4Janus Kinase 1Janus Kinase 3MicePhosphoproteinsPhosphorylationProtein-Tyrosine KinasesReceptors, InterleukinReceptors, Interleukin-4Recombinant Fusion ProteinsAntigens, CDInsulin Receptor Substrate ProteinsInterleukin-4Irs1 protein, mouseJak1 protein, mouseJak3 protein, mouseJanus Kinase 1Janus Kinase 3PhosphoproteinsProtein-Tyrosine KinasesReceptors, InterleukinReceptors, Interleukin-4Recombinant Fusion ProteinsTyrosine

Identifiers

PMID8887542
PMCPMC452180
OpenAlexW2202501092

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.