Evidence map›Paper›PMID 10805787›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction.

J Liao, Y Fu, K Shuai

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 117 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Protein inhibitor of activated STAT1 SerBritish journal of pharmacology · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. CREB SUMOylation by the E3 ligase PIAS1 enhances spatial memory.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  16. Article
  17. Article
  18. The role of hepatic expression of STAT1, SOCS3 and PIAS1 in the response of chronic hepatitis C patients to therapy.Canadian journal of gastroenterology = Journal canadien de gastroenterologie · 2013
    Article
  19. 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

3 authors at 1 institution in 1 country.

J LiaoDivision of Hematology-Oncology, Department of Medicine, University of California, Los Angeles, CA 90095, USA.
Y Fu
K Shuai
University of California, Los Angeles · US

Funding

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
TYROSINE DEPHOSPHORYLATION OF STATS IN IFN SIGNALINGR01AI039612 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SHUAI, KE · 1996 to 2000
$214k
NIAID NIH HHS AI39612NIAID NIH HHS AI43438NIAID NIH HHS R01 AI043438NIAID NIH HHS R21 AI043438
6 · The paper itself

Abstract

STATs are activated by tyrosine phosphorylation on cytokine stimulation. A tyrosine-phosphorylated STAT forms a functional dimer through reciprocal Src homology 2 domain (SH2)-phosphotyrosyl peptide interactions. IFN treatment induces the association of PIAS1 and Stat1, which results in the inhibition of Stat1-mediated gene activation. The molecular basis of the cytokine-dependent PIAS1-Stat1 interaction has not been understood. We report here that a region near the COOH terminus of PIAS1 (amino acids 392-541) directly interacts with the NH(2)-terminal domain of Stat1 (amino acids 1-191). A mutant PIAS1 lacking the Stat1-interacting domain failed to inhibit Stat1-mediated gene activation. By using a modified yeast two-hybrid assay, we demonstrated that PIAS1 specifically interacts with the Stat1 dimer, but not tyrosine-phosphorylated or -unphosphorylated Stat1 monomer. In addition, whereas the NH(2)-terminal region of PIAS1 does not interact with Stat1, it serves as a modulatory domain by preventing the interaction of the COOH-terminal domain of PIAS1 with the Stat1 monomer. Thus, the cytokine-induced PIAS1-Stat1 interaction is mediated through the specific recognition of the dimeric form of Stat1 by PIAS1.

Indexed as

Binding SitesCell LineCloning, MolecularCytokinesDimerizationDNA-Binding ProteinsEscherichia coliGene Expression RegulationHumansProtein Inhibitors of Activated STATProteinsRecombinant ProteinsSaccharomyces cerevisiaeSequence DeletionSignal TransductionSTAT1 Transcription FactorCytokinesDNA-Binding ProteinsProtein Inhibitors of Activated STATProteinsRecombinant ProteinsSTAT1 protein, humanSTAT1 Transcription FactorTrans-Activators

Identifiers

PMID10805787
PMCPMC25817
OpenAlexW1993583458

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.