Evidence map›Paper›PMID 21393235›Full record

ArticleThe Journal of biological chemistry2011

Sts-2 is a phosphatase that negatively regulates zeta-associated protein (ZAP)-70 and T cell receptor signaling pathways.

Boris San Luis, Ben Sondgeroth, Nicolas Nassar, Nick Carpino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. STS2 deficiency revives CD8Journal for immunotherapy of cancer · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. TULA Proteins in Men, Mice, Hens, and Lice: Welcome to the Family.International journal of molecular sciences · 2023
    Review
  16. Review
  17. The Sts Proteins: Modulators of Host Immunity.International journal of molecular sciences · 2023
    Review
  18. UBASH3A Interacts with PTPN22 to RegulateInternational journal of molecular sciences · 2023
    Article
  19. Review
  20. TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022
    Review
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

4 authors at 2 institutions in 2 countries.

Boris San LuisDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794, USA.
Ben Sondgeroth
Nicolas Nassar
Nick Carpino
Laboratory of Molecular Genetics · PLStony 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
Ras, Cycling and Inhibition.R01CA115611 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI NASSAR, NICOLAS · 2007 to 2010
$931k
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
NCI NIH HHS CA-115611NCI NIH HHS R01 CA115611NIAID NIH HHS R01 AI080892NIAID NIH HHS R01AI080892NIAID NIH HHS R21 AI075176NIAID NIH HHS R21AI075176
6 · The paper itself

Abstract

T cell activity is controlled in large part by the T cell receptor (TCR). The TCR detects the presence of foreign pathogens and activates the T cell-mediated immune reaction. Numerous intracellular signaling pathways downstream of the TCR are involved in the process of T cell activation. Negative regulation of these pathways helps prevent excessive and deleterious T cell responses. Two homologous proteins, Sts-1 and Sts-2, have been shown to function as critical negative regulators of TCR signaling. The phosphoglycerate mutase-like domain of Sts-1 (Sts-1(PGM)) has a potent phosphatase activity that contributes to the suppression of TCR signaling. The function of Sts-2(PGM) as a phosphatase has been less clear, principally because its intrinsic enzyme activity has been difficult to detect. Here, we demonstrate that Sts-2 regulates the level of tyrosine phosphorylation on targets within T cells, among them the critical T cell tyrosine kinase Zap-70. Utilizing new phosphorylated substrates, we demonstrate that Sts-2(PGM) has clear, albeit weak, phosphatase activity. We further pinpoint Sts-2 residues Glu-481, Ser-552, and Ser-582 as specificity determinants, in that an Sts-2(PGM) triple mutant in which these three amino acids are altered to their counterparts in Sts-1(PGM) has substantially increased activity. Our results suggest that the phosphatase activities of both suppressor of TCR signaling homologues cooperate in a similar but independent fashion to help set the threshold for TCR-induced T cell activation.

Indexed as

AnimalsCell LineEnzyme ActivationLymphocyte ActivationMiceMice, KnockoutPhosphoprotein PhosphatasesPhosphorylationProtein Tyrosine PhosphatasesReceptors, Antigen, T-CellSignal TransductionSubstrate SpecificityT-LymphocytesZAP-70 Protein-Tyrosine KinasePhosphoprotein PhosphatasesProtein Tyrosine PhosphatasesReceptors, Antigen, T-CellSts-2 protein, mouseTULA-2 protein, mouseZap70 protein, mouseZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID21393235
PMCPMC3091203
OpenAlexW2054704376

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.