Evidence map›Paper›PMID 22084078›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Basic residues in the T-cell receptor ζ cytoplasmic domain mediate membrane association and modulate signaling.

Hao Zhang, Shaun-Paul Cordoba, Omer Dushek, P Anton van der Merwe

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

88 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
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  8. Mechanoregulation of lymphocyte cytotoxicity.Nature reviews. Immunology · 2025
    Review
  9. CD4/CD8-p56Biomolecules · 2025
    Review
  10. Review
  11. Review
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  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Self-programmed dynamics of T cell receptor condensation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

28 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Hao ZhangThe Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Shaun-Paul Cordoba
Omer Dushek
P Anton van der Merwe
University of Oxford · GB

Funding

Medical Research Council G19/31Medical Research Council G9722488Medical Research Council MR/J002011/1
6 · The paper itself

Abstract

The T-cell receptor (TCR) consists of a TCRαβ heterodimer, a TCRζ homodimer, and CD3γε and CD3δε heterodimers. The precise mechanism of T-cell triggering following TCR ligand engagement remains elusive. Previous studies reported that the cytoplasmic tail of CD3ε binds to the plasma membrane through a basic residue-rich stretch (BRS) and proposed that dissociation from the membrane is required for phosphorylation thereof. In this report we show that BRS motifs within the cytoplasmic tail of TCRζ mediate association with the plasma membrane and that TCR engagement results in TCRζ dissociation from the membrane. This dissociation requires phosphorylation of the TCRζ immunoreceptor tyrosine-based activation motifs by lymphocyte cell-specificprotein tyrosine kinase (Lck) but not ζ-chain-associated protein kinase 70 binding. Mutations of the TCRζ BRS motifs that disrupt this membrane association attenuate proximal and distal responses induced by TCR engagement. These mutations appear to alter the localization of TCRζ with respect to Lck as well as the mobility of the TCR complex. This study reveals that tyrosine phosphorylation of the TCRζ cytoplasmic domain regulates its association with the plasma membrane and highlights the functional importance of TCRζ BRS motifs.

Indexed as

Amino Acid MotifsAnimalsBlotting, WesternCell LineCell MembraneCytoplasmFlow CytometryFluorescence Resonance Energy TransferImmunoprecipitationLymphocyte Specific Protein Tyrosine Kinase p56(lck)MiceMicroscopy, ConfocalMutationPhosphorylationReceptors, Antigen, T-CellSignal Transductionantigen T cell receptor, zeta chainLymphocyte Specific Protein Tyrosine Kinase p56(lck)Receptors, Antigen, T-CellTyrosine

Identifiers

PMID22084078
PMCPMC3228420
OpenAlexW1973709420

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.