Evidence map›Paper›PMID 18614237›Full record

ArticleMolecular immunology2008

The protein tyrosine phosphatase PTPN4/PTP-MEG1, an enzyme capable of dephosphorylating the TCR ITAMs and regulating NF-kappaB, is dispensable for T cell development and/or T cell effector functions.

Jennifer A Young, Amy M Becker, Jennifer J Medeiros, Virginia S Shapiro, Andrew Wang, J David Farrar, Timothy A Quill, Rob Hooft van Huijsduijnen, Nicolai S C van Oers

Open access · greenAbstract read
In one paragraph

Article in Molecular immunology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  8. Review
  9. Review
  10. Automatic Bayesian Weighting for SAXS Data.Frontiers in molecular biosciences · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. PTPN4 negatively regulates CrkI in human cell lines.Cellular & molecular biology letters · 2013
    Article
  17. Article
  18. Article
  19. Identification and functional analyses of 11,769 full-length human cDNAs focused on alternative splicing.DNA research : an international journal for rapid publication of reports on genes and genomes · 2009
    Article
  20. 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

9 authors at 3 institutions in 2 countries.

Jennifer A YoungDepartment of Immunology, The University of Texas Southwestern Medical Center, Dallas, TX 75390, United States.
Amy M Becker
Jennifer J Medeiros
Virginia S Shapiro
Andrew Wang
J David Farrar
Timothy A Quill
Rob Hooft van Huijsduijnen
Nicolai S C van Oers
The University of Texas Southwestern Medical Center · USMerck Serono (Switzerland) · CHUniversity of Pennsylvania · US

Funding

INTEGRATIVE IMMUNOLOGY TRAINING PROGRAMT32AI005284 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI Nan Yan · 2003 to 2026
$7.4M
T CELL RECEPTOR SIGNALING BY PHOSPHORYLATED FORMS OF TCRR01AI042953 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI VAN OERS, NICOLAI STANISLAS CYRILLE · 1999 to 2008
$2.4M
PTPN4 Functions in LymphocytesR21AI069249 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI VAN OERS, NICOLAI STANISLAS CYRILLE · 2008 to 2009
$432k
NIAID NIH HHS 5T32AI005284NIAID NIH HHS AI42953NIAID NIH HHS AI69249NIAID NIH HHS R01 AI042953NIAID NIH HHS R21 AI069249NIAID NIH HHS T32 AI005284
6 · The paper itself

Abstract

T cell receptor signaling processes are controlled by the integrated actions of families of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPases). Several distinct cytosolic protein tyrosine phosphatases have been described that are able to negatively regulate TCR signaling pathways, including SHP-1, SHP-2, PTPH1, and PEP. Using PTPase substrate-trapping mutants and wild type enzymes, we determined that PTPN4/PTP-MEG1, a PTPH1-family member, could complex and dephosphorylate the ITAMs of the TCR zeta subunit. In addition, the substrate-trapping derivative augmented basal and TCR-induced activation of NF-kappaB in T cells. To characterize the contribution of this PTPase in T cells, we developed PTPN4-deficient mice. T cell development and TCR signaling events were comparable between wild type and PTPN4-deficient animals. The magnitude and duration of TCR-regulated ITAM phosphorylation, as well as overall protein phosphorylation, was unaltered in the absence of PTPN4. Finally, Th1- and Th2-derived cytokines and in vivo immune responses to Listeria monocytogenes were equivalent between wild type and PTPN4-deficient mice. These findings suggest that additional PTPases are involved in controlling ITAM phosphorylations.

Indexed as

AnimalsCell LineChlorocebus aethiopsCOS CellsHumansJurkat CellsKidneyMiceNF-kappa BProtein Tyrosine Phosphatase, Non-Receptor Type 4Receptors, Antigen, T-CellT-LymphocytesTransfectionNF-kappa BProtein Tyrosine Phosphatase, Non-Receptor Type 4PTPN4 protein, humanReceptors, Antigen, T-Cell

Identifiers

PMID18614237
PMCPMC2596642
OpenAlexW2116206171

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.