Evidence map›Paper›PMID 12138178›Full record

ArticleMolecular and cellular biology2002

Identification of a nuclear Stat1 protein tyrosine phosphatase.

Johanna ten Hoeve, Maria de Jesus Ibarra-Sanchez, Yubin Fu, Wei Zhu, Michel Tremblay, Michael David, Ke Shuai

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 222 papers.

0numbers the graph read from it
0cells of the map it votes in
222citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

222 citing papers in PubMed, 498 citations in OpenAlex.

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  12. Inflammation in glomerular diseases.Frontiers in immunology · 2025
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162 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Johanna ten HoeveDepartment of Medicine, University of California-Los Angeles, Los Angeles, California 90095, USA.
Maria de Jesus Ibarra-Sanchez
Yubin Fu
Wei Zhu
Michel Tremblay
Michael David
Ke Shuai
McGill University · CAUniversity of California, San Diego · USUniversity of California, Los Angeles · US

Funding

INTRACELLULAR SIGNALING BY INTERFERONSR01CA080105 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DAVID, MICHAEL · 1999 to 2006
$1.7M
INHIBITION OF CYTOKINE SIGNALING BY PIS PROTEINSR01AI043438 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SHUAI, KE · 1998 to 2002
$756k
Regulation of Cytokine Signaling by PIAS ProteinR21AI043438 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SHUAI, KE · 2004 to 2004
$307k
NCI NIH HHS CA 80105NIAID NIH HHS AI43438NIAID NIH HHS R01 AI043438NIAID NIH HHS R21 AI043438
6 · The paper itself

Abstract

Upon interferon (IFN) stimulation, Stat1 becomes tyrosine phosphorylated and translocates into the nucleus, where it binds to DNA to activate transcription. The activity of Stat1 is dependent on tyrosine phosphorylation, and its inactivation in the nucleus is accomplished by a previously unknown protein tyrosine phosphatase (PTP). We have now purified a Stat1 PTP activity from HeLa cell nuclear extract and identified it as TC45, the nuclear isoform of the T-cell PTP (TC-PTP). TC45 can dephosphorylate Stat1 both in vitro and in vivo. Nuclear extracts lacking TC45 fail to dephosphorylate Stat1. Furthermore, the dephosphorylation of IFN-induced tyrosine-phosphorylated Stat1 is defective in TC-PTP-null mouse embryonic fibroblasts (MEFs) and primary thymocytes. Reconstitution of TC-PTP-null MEFs with TC45, but not the endoplasmic reticulum (ER)-associated isoform TC48, rescues the defect in Stat1 dephosphorylation. The dephosphorylation of Stat3, but not Stat5 or Stat6, is also affected in TC-PTP-null cells. Our results identify TC45 as a PTP responsible for the dephosphorylation of Stat1 in the nucleus.

Indexed as

AnimalsCell FractionationCell LineDNA-Binding ProteinsEnzyme InhibitorsFibroblastsHumansInterferon-gammaInterleukin-2IsoenzymesMiceNuclear ProteinsPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine PhosphatasesSignal TransductionDNA-Binding ProteinsEnzyme InhibitorsInterferon-gammaInterleukin-2IsoenzymesNuclear ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine PhosphatasesPTPN2 protein, humanPtpn2 protein, mouseSTAT1 protein, humanStat1 protein, mouseSTAT1 Transcription FactorStaurosporineTrans-Activators

Identifiers

PMID12138178
PMCPMC133976
OpenAlexW2147511779

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.