Evidence map›Paper›PMID 20965228›Full record

ArticleMolecular and cellular endocrinology2011

Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation.

Natalia Varlakhanova, Johnnie B Hahm, Martin L Privalsky

Abstract read
In one paragraph

Article in Molecular and cellular endocrinology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. BQ323636.1, a Novel Splice Variant toClinical cancer research : an official journal of the American Association for Cancer Research · 2018
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Nuclear hormone receptor co-repressors: structure and function.Molecular and cellular endocrinology · 2012
    Review
  13. Article
  14. Article
  15. Article
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.

Natalia VarlakhanovaDepartment of Microbiology, College of Biological Sciences, University of California at Davis, United States.
Johnnie B Hahm
Martin L Privalsky
University of California, Davis · US

Funding

Role of cofactors in nuclear hormone receptor function.R01DK053528 · NIDDK · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1998 to 2012
$2.9M
NIDDK NIH HHS R01 DK053528NIDDK NIH HHS R01DK53528
6 · The paper itself

Abstract

The SMRT (Silencing Mediator of Retinoid and Thyroid hormone receptors) corepressor mediates gene repression by nuclear receptors and other transcriptional factors. The SMRT protein serves as a key nucleating core that organizes the assembly of a larger corepressor complex. We report here that SMRT interacts with itself to form a protein dimer, and that Erk2, a mitogen-activated protein (MAP) kinase, disrupts this SMRT self-dimerization in vitro and in vivo. Notably Erk2 phosphorylation also results in a re-organization of the overall corepressor complex, characterized by a reduced sedimentation coefficient, partial release of HDAC3, TBL-1, and TBLR-1, and inhibition of transcriptional repression. We propose that SMRT dimers form the central platform on which additional corepressor components assemble, and that kinase signaling modifies the architecture, composition, and function of this complex. These observations contribute to our understanding of how the SMRT corepressor complex assembles and is regulated during cell proliferation and differentiation.

Indexed as

Protein Structure, QuaternaryAnimalsDimerizationHumansMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesMultiprotein ComplexesNuclear Receptor Co-Repressor 2PhosphorylationRecombinant Fusion ProteinsSignal TransductionMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesMultiprotein ComplexesNuclear Receptor Co-Repressor 2Recombinant Fusion Proteins

Identifiers

PMID20965228
PMCPMC3011023
OpenAlexW2061319093

What OpenQuestion holds

Textmetadata
LicenceTDM
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.