Evidence map›Paper›PMID 18829468›Full record

ArticleThe Journal of biological chemistry2008

Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the gamma chain.

Yaniv Malka, Tekla Hornakova, Yohan Royer, Laurent Knoops, Jean-Christophe Renauld, Stefan N Constantinescu, Yoav I Henis

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. IL-2 receptors preassemble and signal in the ER/Golgi causing resistance to antiproliferative anti-IL-2Rα therapies.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Review
  9. Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells: A quantitative CLSM and FRET analysis.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2018
    Article
  10. Review
  11. IL-7 Induces an Epitope Masking ofMediators of inflammation · 2017
    Article
  12. Review
  13. The common γ-chain cytokine receptor: tricks-and-treats for T cells.Cellular and molecular life sciences : CMLS · 2016
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Structural reorganization of the interleukin-7 signaling complex.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

7 authors at 3 institutions in 2 countries.

Yaniv MalkaDepartment of Neurobiology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Tekla Hornakova
Yohan Royer
Laurent Knoops
Jean-Christophe Renauld
Stefan N Constantinescu
Yoav I Henis
de Duve Institute · BELudwig Cancer Research · BETel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signaling via interleukin-2 (IL-2) and interleukin-9 receptors (IL-2R and IL-9R) involves heteromeric interactions between specific interleukin receptor subunits, which bind Janus kinase 1 (JAK1) and the JAK3 binding common gamma chain (gamma c). The potential existence and roles of homomeric and heteromeric complexes before ligand binding and their modulation by ligand and JAK3 are unclear. Using computerized antibody-mediated immunofluorescence co-patching of epitope-tagged receptors at the surface of live cells, we demonstrate that IL-2Rbeta, IL-9Ralpha, and gamma c each display a significant fraction of ligand-independent homomeric complexes (24-28% co-patching), whereas control co-patching levels with unrelated receptors are very low (7%). Heteromeric complex formation of IL2-Rbeta or IL-9Ralpha with gamma c is also observed in the absence of ligand (15-30%). Ligand binding increases this hetero-oligomerization 2-fold but does not affect homo-oligomerization. Co-expression of IL-2Ralpha does not affect the hetero-oligomerization of IL-2Rbeta and gamma c. Recruitment of gamma c into heterocomplexes is partly at the expense of its homo-oligomerization, suggesting that a functional role of the latter may be to keep the receptors inactive in the absence of ligand. At the same time, the preformed complexes between gamma c and IL-2Rbeta or IL-9Ralpha promote signaling by the JAK3 A572V mutant without ligand, supporting a pathophysiological role for the constitutive oligomerization in triggering ligand-independent activation of JAK3 (and perhaps other JAK mutants) mutants identified in several human cancers.

Indexed as

Signal TransductionAmino Acid SubstitutionHumansInterleukin-2 Receptor alpha SubunitInterleukin-2 Receptor beta SubunitInterleukin Receptor Common gamma SubunitJanus Kinase 1Janus Kinase 3LigandsMultiprotein ComplexesMutation, MissenseNeoplasmsReceptors, Interleukin-9IL2RA protein, humanIL2RB protein, humanIL2RG protein, humanIL9R protein, humanInterleukin-2 Receptor alpha SubunitInterleukin-2 Receptor beta SubunitInterleukin Receptor Common gamma SubunitJAK1 protein, humanJAK3 protein, humanJanus Kinase 1Janus Kinase 3LigandsMultiprotein ComplexesReceptors, Interleukin-9

Identifiers

PMID18829468
PMCPMC2662275
OpenAlexW2069338504

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.