Evidence map›Paper›PMID 18320063›Full record

ArticlePloS one2008

T cell receptor engagement triggers its CD3epsilon and CD3zeta subunits to adopt a compact, locked conformation.

Ruth M Risueño, Wolfgang W A Schamel, Balbino Alarcón

Abstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. Direct Regulation of the T Cell Antigen Receptor's Activity by Cholesterol.Frontiers in cell and developmental biology · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Meeting report: Signal transduction meets systems biology.Cell communication and signaling : CCS · 2012
    Article
  11. Article
  12. Basic residues in the T-cell receptor ζ cytoplasmic domain mediate membrane association and modulate signaling.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Mechanisms for T cell receptor triggering.Nature reviews. Immunology · 2011
    Review
  14. Article
  15. Nck adapter proteins: functional versatility in T cells.Cell communication and signaling : CCS · 2009
    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

3 authors.

Ruth M RisueñoCentro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Madrid, Spain.
Wolfgang W A Schamel
Balbino Alarcón

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How the T cell antigen receptor (TCR) discriminates between molecularly related peptide/Major Histocompatibility Complex (pMHC) ligands and converts this information into different possible signaling outcomes is still not understood. One current model proposes that strong pMHC ligands, but not weak ones, induce a conformational change in the TCR. Evidence supporting this comes from a pull-down assay that detects ligand-induced binding of the TCR to the N-terminal SH3 domain of the adapter protein Nck, and also from studies with a neoepitope-specific antibody. Both methods rely on the exposure of a polyproline sequence in the CD3epsilon subunit of the TCR, and neither indicates whether the conformational change is transmitted to other CD3 subunits. Using a protease-sensitivity assay, we now show that the cytoplasmic tails of CD3epsilon and CD3zeta subunits become fully protected from degradation upon TCR triggering. These results suggest that the TCR conformational change is transmitted to the tails of CD3epsilon and CD3zeta, and perhaps all CD3 subunits. Furthermore, the resistance to protease digestion suggests that CD3 cytoplasmic tails adopt a compact structure in the triggered TCR. These results are consistent with a model in which transduction of the conformational change induced upon TCR triggering promotes condensation and shielding of the CD3 cytoplasmic tails.

Indexed as

Adaptor Proteins, Signal TransducingCD3 ComplexHumansJurkat CellsMajor Histocompatibility ComplexOncogene ProteinsPeptide FragmentsProtein ConformationReceptor-CD3 Complex, Antigen, T-CellT-LymphocytesAdaptor Proteins, Signal TransducingCD3 antigen, zeta chainCD3 ComplexCD3E protein, humanNck proteinOncogene ProteinsPeptide FragmentsReceptor-CD3 Complex, Antigen, T-Cell

Identifiers

PMID18320063
PMCPMC2254190

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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.