Evidence map›Paper›PMID 10454532›Full record

ArticleMolecular and cellular biology1999

Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte.

D Vermaak, P A Wade, P L Jones, Y B Shi, A P Wolffe

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of miR-6794-3p as a suppressor in pancreatic cancer metastasis.International journal of biological sciences · 2024
    Article
  4. RBBP4 promotes colon cancer malignant progressionWorld journal of gastroenterology · 2020
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Characterization of the expression pattern of the PRC2 core subunit Suz12 during embryonic development of Xenopus laevis.Developmental dynamics : an official publication of the American Association of Anatomists · 2009
    Article
  18. Review
  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

5 authors at 2 institutions in 1 country.

D VermaakLaboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-5431, USA.
P A Wade
P L Jones
Y B Shi
A P Wolffe
National Institutes of Health · USEunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Molecular mechanism of thyroid hormone receptor function during metamorphosisZIAHD001901 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SHI, YUN-BO · 2009 to 2025
$13.1M
Molecular mechanism of thyroid hormone receptor function during metamorphosisZ01HD001901 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SHI, YUN-BO · 1995 to 2008
$2.1M
6 · The paper itself

Abstract

We investigated the protein associations and enzymatic requirements for the Xenopus histone deacetylase catalytic subunit RPD3 to direct transcriptional repression in Xenopus oocytes. Endogenous Xenopus RPD3 is present in nuclear and cytoplasmic pools, whereas RbAp48 and SIN3 are predominantly nuclear. We cloned Xenopus RbAp48 and SIN3 and show that expression of RPD3, but not RbAp48 or SIN3, leads to an increase in nuclear and cytoplasmic histone deacetylase activity and transcriptional repression of the TRbetaA promoter. This repression requires deacetylase activity and nuclear import of RPD3 mediated by a carboxy-terminal nuclear localization signal. Exogenous RPD3 is not incorporated into previously described oocyte deacetylase and ATPase complexes but cofractionates with a component of the endogenous RbAp48 in the oocyte nucleus. We show that RPD3 associates with RbAp48 through N- and C-terminal contacts and that RbAp48 also interacts with SIN3. Xenopus RbAp48 selectively binds to the segment of the N-terminal tail immediately proximal to the histone fold domain of histone H4 in vivo. Exogenous RPD3 may be targeted to histones through interaction with endogenous RbAp48 to direct transcriptional repression of the Xenopus TRbetaA promoter in the oocyte nucleus. However, the exogenous RPD3 deacetylase functions to repress transcription in the absence of a requirement for association with SIN3 or other targeted corepressors.

Indexed as

Repressor ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell NucleusCloning, MolecularCytoplasmDNA PrimersFemaleHistone DeacetylasesHistonesHumansIn Vitro TechniquesMacromolecular SubstancesCarrier ProteinsDNA PrimersHistone DeacetylasesHistonesMacromolecular SubstancesNuclear ProteinsRBBP4 protein, humanRepressor ProteinsRetinoblastoma-Binding Protein 4Saccharomyces cerevisiae ProteinsSIN3A protein, XenopusSIN3 protein, S cerevisiaeTranscription Factors

Identifiers

PMID10454532
PMCPMC84434
OpenAlexW2168359916

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.