Evidence map›Paper›PMID 26043137›Full record

ArticleJournal of proteome research2015

Vav1 Regulates T-Cell Activation through a Feedback Mechanism and Crosstalk between the T-Cell Receptor and CD28.

Ynes A Helou, Anna P Petrashen, Arthur R Salomon

Abstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Role of Protein Methyltransferases in Immunity.Molecules (Basel, Switzerland) · 2024
    Review
  6. CD4Epigenetics · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
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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 at 1 institution in 1 country.

Ynes A Helou†Department of Molecular Pharmacology, Physiology, and Biotechnology and ‡Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02903, United States.
Anna P Petrashen†Department of Molecular Pharmacology, Physiology, and Biotechnology and ‡Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02903, United States.
Arthur R Salomon†Department of Molecular Pharmacology, Physiology, and Biotechnology and ‡Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02903, United States.
Brown University · US

Funding

Phosphoproteomic Analysis of T Cell Activation PathwaysR01AI083636 · NIAID · BROWN UNIVERSITY · PI SALOMON, ARTHUR ROBERT · 2010 to 2021
$4.0M
Predoctoral Training in the Molecular Biology of AgingT32AG041688 · NIA · BROWN UNIVERSITY · PI NICOLA NERETTI, John M Sedivy · 2012 to 2026
$3.5M
Acquisition of an Orbitrap XL ETD Mass Spectrometer through Upgrading an LTQS10RR027027 · NCRR · BROWN UNIVERSITY · PI HAWROT, EDWARD · 2010 to 2010
$500k
NCRR NIH HHS S10 RR027027NIAID NIH HHS R01 AI083636NIA NIH HHS T32 AG041688
6 · The paper itself

Abstract

Vav1, a Rac/Rho guanine nucleotide exchange factor and a critical component of the T-cell receptor (TCR) signaling cascade is tyrosine phosphorylated rapidly in response to T-cell activation. Vav1 has established roles in proliferation, cytokine secretion, Ca(2+) responses, and actin cytoskeleton regulation; however, its function in the regulation of phosphorylation of TCR components, including the ζ chain, the CD3 δ, ε, γ chains, and the associated kinases Lck and ZAP-70, is not well established. To obtain a more comprehensive picture of the role of Vav1 in receptor proximal signaling, we performed a wide-scale characterization of Vav1-dependent tyrosine phosphorylation events using quantitative phosphoproteomic analysis of Vav1-deficient T cells across a time course of TCR stimulation. Importantly, this study revealed a new function for Vav1 in the negative feedback regulation of the phosphorylation of immunoreceptor tyrosine-based activation motifs within the ζ chains, CD3 δ, ε, γ chains, as well as activation sites on the critical T cell tyrosine kinases Itk, Lck, and ZAP-70. Our study also uncovered a previously unappreciated role for Vav1 in crosstalk between the CD28 and TCR signaling pathways.

Indexed as

Receptor Cross-TalkCD28 AntigensHumansJurkat CellsLymphocyte ActivationPhosphatidylinositol 3-KinasesPhosphorylationProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellSignal TransductionT-LymphocytesZAP-70 Protein-Tyrosine KinaseCD28 AntigensPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-vavReceptors, Antigen, T-CellVAV1 protein, humanZAP70 protein, humanZAP-70 Protein-Tyrosine Kinasemass spectrometryphosphoproteomicsT cell receptor signalingVav1

Identifiers

PMID26043137
PMCPMC4490005
OpenAlexW2412418425

What Socratic 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 Socratic graph.