Evidence map›Paper›PMID 27354065›Full record

ArticleMolecular and cellular biology2016

Phosphorylation of a Tyrosine Residue on Zap70 by Lck and Its Subsequent Binding via an SH2 Domain May Be a Key Gatekeeper of T Cell Receptor Signaling In Vivo.

Peter A Thill, Arthur Weiss, Arup K Chakraborty

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  5. Endosome Traffic Modulates Pro-Inflammatory Signal Transduction in CD4International journal of molecular sciences · 2023
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  13. CAR- and TRuC-redirected regulatory T cells differ in capacity to control adaptive immunity to FVIII.Molecular therapy : the journal of the American Society of Gene Therapy · 2021
    Article
  14. Review
  15. Article
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  17. Article
  18. Article
  19. Review
  20. How the T cell signaling network processes information to discriminate between self and agonist ligands.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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 at 2 institutions in 1 country.

Peter A ThillDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Arthur WeissRosalind Russell/Ephraim P. Engleman Rheumatology Research Center, Division of Rheumatology, Department of Medicine, University of California at San Francisco, San Francisco, California, USA Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, California, USA aweiss@medicine.ucsf.edu arupc@mit.edu.
Arup K ChakrabortyDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA Department of Physics, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA Institute for Medical Engineering and Science, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA Ragon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, USA aweiss@medicine.ucsf.edu arupc@mit.edu.
Massachusetts Institute of Technology · USHoward Hughes Medical Institute · US

Funding

Understand the metabolic fitness of naïve T cellsP01AI091580 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ARTHUR WEISS · 2011 to 2026
$31.1M
NIAID NIH HHS P01 AI091580
6 · The paper itself

Abstract

The initiation of signaling in T lymphocytes in response to the binding of the T cell receptor (TCR) to cognate ligands is a key step in the emergence of adaptive immune responses. Conventional models posit that TCR signaling is initiated by the phosphorylation of receptor-associated immune receptor activation motifs (ITAMs). The cytoplasmic tyrosine kinase Zap70 binds to phosphorylated ITAMs, is subsequently activated, and then propagates downstream signaling. While evidence for such models is provided by experiments with cell lines, in vivo, Zap70 is bound to phosphorylated ITAMs in resting T cells. However, Zap70 is activated only upon TCR binding to cognate ligand. We report the results of computational studies of a new model for the initiation of TCR signaling that incorporates these in vivo observations. Importantly, the new model is shown to allow better and faster TCR discrimination between self-ligands and foreign ligands. The new model is consistent with many past experimental observations, and experiments that could further test the model are proposed.

Indexed as

Binding SitesComputer SimulationLymphocyte Specific Protein Tyrosine Kinase p56(lck)Models, MolecularPhosphorylationProtein BindingReceptors, Antigen, T-CellSignal TransductionTyrosineZAP-70 Protein-Tyrosine KinaseLymphocyte Specific Protein Tyrosine Kinase p56(lck)Receptors, Antigen, T-CellTyrosineZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID27354065
PMCPMC5007795
OpenAlexW2471277463

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.