Evidence map›Paper›PMID 17130234›Full record

ArticleMolecular and cellular biology2007

Caspase-3 regulates catalytic activity and scaffolding functions of the protein tyrosine phosphatase PEST, a novel modulator of the apoptotic response.

Maxime Hallé, Ying-Chih Liu, Serge Hardy, Jean-François Théberge, Christophe Blanchetot, Annie Bourdeau, Tzu-Ching Meng, Michel L Tremblay

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Fas ligand intracellular signaling: does PSTPIP mediate T cell death?Apoptosis : an international journal on programmed cell death · 2024
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  5. Review
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  9. Review
  10. SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis.Cellular & molecular biology letters · 2012
    Article
  11. 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

8 authors at 3 institutions in 3 countries.

Maxime HalléInstitute of Biological Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nankang 115, Taipei, Taiwan.
Ying-Chih Liu
Serge Hardy
Jean-François Théberge
Christophe Blanchetot
Annie Bourdeau
Tzu-Ching Meng
Michel L Tremblay
McGill University · CAInstitute of Biological Chemistry, Academia Sinica · TWUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein tyrosine phosphatase PEST (PTP-PEST) is involved in the regulation of the actin cytoskeleton. Despite the emerging functions attributed to both PTPs and the actin cytoskeleton in apoptosis, the involvement of PTP-PEST in apoptotic cell death remains to be established. Using several cell-based assays, we showed that PTP-PEST participates in the regulation of apoptosis. As apoptosis progressed, a pool of PTP-PEST localized to the edge of retracting lamellipodia. Expression of PTP-PEST also sensitized cells to receptor-mediated apoptosis. Concertedly, specific degradation of PTP-PEST was observed during apoptosis. Pharmacological inhibitors, immunodepletion experiments, and in vitro cleavage assays identified caspase-3 as the primary regulator of PTP-PEST processing during apoptosis. Caspase-3 specifically cleaved PTP-PEST at the (549)DSPD motif and generated fragments, some of which displayed increased catalytic activity. Moreover, caspase-3 regulated PTP-PEST interactions with paxillin, leupaxin, Shc, and PSTPIP. PTP-PEST acted as a scaffolding molecule connecting PSTPIP to additional partners: paxillin, Shc, Csk, and activation of caspase-3 correlated with the modulation of the PTP-PEST adaptor function. In addition, cleavage of PTP-PEST facilitated cellular detachment during apoptosis. Together, our data demonstrate that PTP-PEST actively contributes to the cellular apoptotic response and reveal the importance of caspases as regulators of PTPs in apoptosis.

Indexed as

ApoptosisAmino Acid SequenceAnimalsCaspase 3CatalysisCell Surface ExtensionsCell SurvivalEnzyme ActivationHeLa CellsHumansMiceMolecular Sequence DataProtein BindingProtein Processing, Post-TranslationalProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 12Caspase 3Protein Tyrosine Phosphatase, Non-Receptor Type 12Protein Tyrosine PhosphatasesPTPN12 protein, humanPtpn12 protein, mouseRecombinant Fusion Proteins

Identifiers

PMID17130234
PMCPMC1800677
OpenAlexW2154474746

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.