Evidence map›Paper›PMID 16611580›Full record

ReviewMolecular membrane biology

Lipid rafts in T cell receptor signalling .

Panagiotis S Kabouridis

Open access · greenAbstract readReview
In one paragraph

Review in Molecular membrane biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
5.5field-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

69 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
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  9. Article
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  11. Significance of Receptor Mobility in Multivalent Binding on Lipid Membranes.Angewandte Chemie (International ed. in English) · 2022
    Review
  12. Review
  13. Article
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  15. Article
  16. Article
  17. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  18. How the Discovery of the CD4/CD8-p56Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. Review

9 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

1 author at 1 institution in 1 country.

Panagiotis S KabouridisBone & Joint Research Unit, William Harvey Research Institute, Queen Mary's School of Medicine & Dentistry, University of London, UK. p.skabouridis@qmul.ac.uk
University of London · GB

Funding

Arthritis Research UK 16018Wellcome Trust 058408
6 · The paper itself

Abstract

The molecular events and the protein components that are involved in signalling by the T cell receptor (TCR) for antigen have been extensively studied. Activation of signalling cascades following TCR stimulation depends on the phosphorylation of the receptor by the tyrosine kinase Lck, which localizes to the cytoplasmic face of the plasma membrane by virtue of its post-translational modification. However, the precise order of events during TCR phosphorylation at the plasma membrane, remains to be defined. A current theory that describes early signalling events incorporates the function of lipid rafts, microdomains at the plasma membrane with distinct lipid and protein composition. Lipid rafts have been implicated in diverse biological functions in mammalian cells. In T cells, molecules with a key role in TCR signalling, including Lck, localize to these domains. Importantly, mutant versions of these proteins which fail to localise to raft domains were unable to support signalling by the TCR. Biochemical studies using purified detergent-resistant membranes (DRM) and confocal microscopy have suggested that upon stimulation, the TCR and Lck-containing lipid rafts may come into proximity allowing phosphorylation of the receptor. Further, there are data suggesting that phosphorylation of the TCR could depend on a transient increase in Lck activity that takes place within lipid rafts to initiate signalling. Current results and a model of how lipid rafts may regulate TCR signalling are discussed.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane MicrodomainsModels, ImmunologicalPhosphorylationReceptors, Antigen, T-CellSignal TransductionT-LymphocytesAdaptor Proteins, Signal TransducingLymphocyte Specific Protein Tyrosine Kinase p56(lck)Receptors, Antigen, T-Cell

Identifiers

PMID16611580
PMCPMC2596298
OpenAlexW2028457751

What OpenQuestion holds

Textmetadata
LicenceTDM
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.