Evidence map›Paper›PMID 24256567›Full record

ArticleThe FEBS journal2014

Insights into the suppressor of T-cell receptor (TCR) signaling-1 (Sts-1)-mediated regulation of TCR signaling through the use of novel substrate-trapping Sts-1 phosphatase variants.

Boris S Luis, Nick Carpino

Abstract read
In one paragraph

Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  5. TULA Proteins in Men, Mice, Hens, and Lice: Welcome to the Family.International journal of molecular sciences · 2023
    Review
  6. TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022
    Review
  7. Review
  8. 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

2 authors at 1 institution in 1 country.

Boris S LuisProgram in Molecular and Cellular Biology, Stony Brook University, NY, USA.
Nick Carpino
Stony Brook University · US

Funding

Regulation of TCR Signaling by Sts-1 and Sts-2R01AI080892 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI CARPINO, NICHOLAS A · 2010 to 2014
$1.9M
Regulation of TCR signaling by a novel enzyme activity.R21AI075176 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI CARPINO, NICHOLAS A · 2007 to 2008
$422k
NIAID NIH HHS R01 AI080892NIAID NIH HHS R01AI080892NIAID NIH HHS R21 AI075176NIAID NIH HHS R21AI075176
6 · The paper itself

Abstract

High affinity substrate-trapping protein tyrosine phosphatases have been widely used both to investigate the endogenous targets of many phosphatases and to address questions of substrate specificity. Herein, we extend the concept of a substrate-trapping phosphatase to include an enzyme of the histidine phosphatase superfamily. This is the first description of substrate-trapping technology applied to a member of the histidine phosphatase family. The phosphatase suppressor of T-cell receptor signaling (Sts)-1 has recently been reported to negatively regulate signaling downstream of the T-cell receptor. We generated high-affinity substrate-trapping variants of Sts-1 by mutagenesis of key active site residues within the phosphatase catalytic domain. Mutation of both the nucleophilic His380 and the general acid Glu490 yielded Sts-1 enzymes that were catalytically inactive but showed high affinity for an important tyrosine kinase in T cells that Sts-1 is known to regulate, Zap-70. Sts-1 substrate-trapping mutants isolated tyrosine-phosphorylated Zap-70 from lysates of activated T cells, validating Zap-70 as a possible substrate for Sts-1 and highlighting the efficacy of the mutants as substrate-trapping agents. Inhibition of the Zap-70 interaction by vanadate suggests that the substrate-trapping effect occurred via the Sts-1 phosphatase active site. Finally, overexpression of Sts-1 substrate-trapping mutants in T cells blocked T-cell receptor signaling, confirming the inhibitory effect of Sts-1 on Zap-70.

Indexed as

Lymphocyte ActivationSignal TransductionAmino Acid SubstitutionAnimalsCatalytic DomainCell LineCells, CulturedHumansMiceMice, KnockoutMutant ProteinsPeptide FragmentsPhosphorylationProtein Kinase InhibitorsProtein Processing, Post-TranslationalProtein Tyrosine PhosphatasesMutant ProteinsPeptide FragmentsProtein Kinase InhibitorsProtein Tyrosine PhosphatasesReceptors, Antigen, T-CellRecombinant ProteinsTULA-2 protein, mouseZAP70 protein, humanZap70 protein, mouseZAP-70 Protein-Tyrosine Kinasehistidine phosphatase superfamilysuppressor of T-cell receptor signaling (Sts) proteinsT-cell receptor (TCR) signaling

Identifiers

PMID24256567
PMCPMC3968691
OpenAlexW2127525038

What OpenQuestion holds

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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.