Evidence map›Paper›PMID 11432829›Full record

ArticleThe EMBO journal2001

PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates.

D Davidson, A Veillette

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
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

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Regulation of CD4Frontiers in immunology · 2019
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  18. Signaling mechanisms regulating B-lymphocyte activation and tolerance.Journal of molecular medicine (Berlin, Germany) · 2015
    Review
  19. Osteoblast differentiation and migration are regulated by dynamin GTPase activity.The international journal of biochemistry & cell biology · 2014
    Article
  20. 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

2 authors at 1 institution in 2 countries.

D DavidsonLaboratory of Molecular Oncology, IRCM, 110 Pine Avenue West, Montréal, Québec H2W 1R7, Canada.
A Veillette
McGill University Health Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is increasing interest in elucidating the mechanisms involved in the negative regulation of lymphocyte activation. Herein, we show that the cytosolic protein tyrosine phosphatase PTP-PEST is expressed abundantly in a wide variety of haemopoietic cell types, including B cells and T cells. In a model B-cell line, PTP-PEST was found to be constitutively associated with several signalling molecules, including Shc, paxillin, Csk and Cas. The interaction between Shc and PTP-PEST was augmented further by antigen receptor stimulation. Overexpression studies, antisense experiments and structure-function analyses provided evidence that PTP-PEST is an efficient negative regulator of lymphocyte activation. This function correlated with the ability of PTP-PEST to induce dephosphorylation of Shc, Pyk2, Fak and Cas, and inactivate the Ras pathway. Taken together, these data suggest that PTP-PEST is a novel and unique component of the inhibitory signalling machinery in lymphocytes.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsB-LymphocytesCells, CulturedCytoskeletal ProteinsHomeostasisKineticsLymphocyte ActivationMiceMice, Inbred C57BLOligodeoxyribonucleotides, AntisensePaxillinPhosphoproteinsPhosphorylationProteinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCytoskeletal ProteinsOligodeoxyribonucleotides, AntisensePaxillinPhosphoproteinsProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 12Protein Tyrosine PhosphatasesPtpn12 protein, mousePxn protein, mouseras ProteinsRecombinant ProteinsShc1 protein, mouseShc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1

Identifiers

PMID11432829
PMCPMC125513
OpenAlexW2032588409

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.