Evidence map›Paper›PMID 10938135›Full record

ArticleMolecular and cellular biology2000

The SMRT corepressor is regulated by a MEK-1 kinase pathway: inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export.

S H Hong, M L Privalsky

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed, 185 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Regulation of habit formation in the dorsal striatum.Current opinion in behavioral sciences · 2018
    Article
  5. Article
  6. Article
  7. Review
  8. AT1R blockade in adverse milieus: role of SMRT and corepressor complexes.American journal of physiology. Renal physiology · 2015
    Article
  9. Article
  10. Rescue of a primary myelofibrosis model by retinoid-antagonist therapy.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Nuclear hormone receptor co-repressors: structure and function.Molecular and cellular endocrinology · 2012
    Review

2 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

2 authors at 1 institution in 1 country.

S H HongSection of Microbiology, University of California at Davis, Davis, California 95616, USA.
M L Privalsky
University of California, Davis · US

Funding

MECHANISM OF ACTION OF THE VERB A ONCOGENE OF AEVR37CA053394 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1994 to 2012
$3.4M
Role of cofactors in nuclear hormone receptor function.R01DK053528 · NIDDK · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1998 to 2012
$2.9M
NCI NIH HHS R37 CA053394NCI NIH HHS R37 CA-53394NIDDK NIH HHS R01 DK053528NIDDK NIH HHS R01 DK-53528
6 · The paper itself

Abstract

The SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor participates in the repression of target gene expression by a variety of transcription factors, including the nuclear hormone receptors, promyelocytic leukemia zinc finger protein, and B-cell leukemia protein 6. The ability of SMRT to associate with these transcription factors and thereby to mediate repression is strongly inhibited by activation of tyrosine kinase signaling pathways, such as that represented by the epidermal growth factor receptor. We report here that SMRT function is potently inhibited by a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) cascade that operates downstream of this growth factor receptor. Intriguingly, the SMRT protein is a substrate for phosphorylation by protein kinases operating at multiple levels in this MAPKKK pathway, including the MAPKs, MAPK-extracellular signal-regulated kinase 1 (MEK-1), and MEK-1 kinase (MEKK-1). Phosphorylation of SMRT by MEKK-1 and, to a lesser extent, MEK-1 inhibits the ability of SMRT to physically tether to its transcription factor partners. Notably, activation of MEKK-1 or MEK-1 signaling in transfected cells also leads to a redistribution of the SMRT protein from a nuclear compartment to a more perinuclear or cytoplasmic compartment. We suggest that SMRT-mediated repression is regulated by the MAPKKK cascade and that changes both in the affinity of SMRT for its transcription factors and in the subcellular distribution of SMRT contribute to the loss of SMRT function that is observed in response to kinase signal transduction.

Indexed as

MAP Kinase Signaling SystemAnimalsCell LineCell NucleusCOS CellsDNA-Binding ProteinsGenes, erbB-1HaplorhiniImmunoblottingMAP Kinase Kinase 1MAP Kinase Kinase KinasesMicroscopy, ConfocalMitogen-Activated Protein Kinase KinasesModels, BiologicalNuclear Receptor Co-Repressor 2PhosphorylationDNA-Binding ProteinsMAP Kinase Kinase 1MAP Kinase Kinase KinasesMitogen-Activated Protein Kinase KinasesNuclear Receptor Co-Repressor 2Protein Serine-Threonine KinasesProtein-Tyrosine KinasesRepressor Proteins

Identifiers

PMID10938135
PMCPMC86146
OpenAlexW2114334107

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.