Evidence map›Paper›PMID 10790433›Full record

ArticleThe Journal of experimental medicine2000

Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation.

T Brdicka, D Pavlistová, A Leo, E Bruyns, V Korínek, P Angelisová, J Scherer, A Shevchenko, I Hilgert, J Cerný and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

175 citing papers in PubMed, 460 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
  15. Acute Csk inhibition hinders B cell activation by constraining the PI3 kinase pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

115 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

15 authors at 4 institutions in 2 countries.

T BrdickaInstitute of Molecular Genetics, Academy of Sciences of the Czech Republic, 14220 Prague, Czech Republic.
D Pavlistová
A Leo
E Bruyns
V Korínek
P Angelisová
J Scherer
A Shevchenko
I Hilgert
J Cerný
K Drbal
Y Kuramitsu
B Kornacker
V Horejsí
B Schraven
Czech Academy of Sciences, Institute of Molecular Genetics · CZHeidelberg University · DEEuropean Molecular Biology Laboratory · DECharles University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

According to a recently proposed hypothesis, initiation of signal transduction via immunoreceptors depends on interactions of the engaged immunoreceptor with glycosphingolipid-enriched membrane microdomains (GEMs). In this study, we describe a novel GEM-associated transmembrane adaptor protein, termed phosphoprotein associated with GEMs (PAG). PAG comprises a short extracellular domain of 16 amino acids and a 397-amino acid cytoplasmic tail containing ten tyrosine residues that are likely phosphorylated by Src family kinases. In lymphoid cell lines and in resting peripheral blood alpha/beta T cells, PAG is expressed as a constitutively tyrosine-phosphorylated protein and binds the major negative regulator of Src kinases, the tyrosine kinase Csk. After activation of peripheral blood alpha/beta T cells, PAG becomes rapidly dephosphorylated and dissociates from Csk. Expression of PAG in COS cells results in recruitment of endogenous Csk, altered Src kinase activity, and impaired phosphorylation of Src-specific substrates. Moreover, overexpression of PAG in Jurkat cells downregulates T cell receptor-mediated activation of the transcription factor nuclear factor of activated T cells. These findings collectively suggest that in the absence of external stimuli, the PAG-Csk complex transmits negative regulatory signals and thus may help to keep resting T cells in a quiescent state.

Indexed as

Lymphocyte ActivationAdaptor Proteins, Signal TransducingAmino Acid SequenceCD3 ComplexCloning, MolecularCSK Tyrosine-Protein KinaseDNA, ComplementaryGlycosphingolipidsHumansMembrane ProteinsMolecular Sequence DataPhosphoproteinsProtein BindingProtein-Tyrosine KinasesReceptors, Antigen, T-CellSignal TransductionAdaptor Proteins, Signal TransducingCD3 ComplexCSK protein, humanCSK Tyrosine-Protein KinaseDNA, ComplementaryGlycosphingolipidsMembrane ProteinsPAG1 protein, humanPhosphoproteinsProtein-Tyrosine KinasesReceptors, Antigen, T-Cellsrc-Family Kinases

Identifiers

PMID10790433
PMCPMC2213442
OpenAlexW2160675888

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.