Evidence map›Paper›PMID 14522945›Full record

ArticleGenes & development2003

mSin3-associated protein, mSds3, is essential for pericentric heterochromatin formation and chromosome segregation in mammalian cells.

Gregory David, Garth M Turner, Yao Yao, Alexei Protopopov, Ronald A DePinho

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Sin3a regulates the developmental progression through morula-to-blastocyst transitionFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  5. Article
  6. Article
  7. Review
  8. Zebrafish sin3b mutants are viable but have size, skeletal, and locomotor defects.Developmental dynamics : an official publication of the American Association of Anatomists · 2017
    Article
  9. Article
  10. 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
  11. Article
  12. Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Review
  14. Article
  15. Article
  16. Article
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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.

Gregory DavidDepartments of Medical Oncology, Medicine, and Genetics, Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, USA.
Garth M Turner
Yao Yao
Alexei Protopopov
Ronald A DePinho
Harvard University · USDana-Farber Cancer Institute · US

Funding

MYC NETWORK FUNCTION IN DEVELOPMENTR01CA086379 · NCI · DANA-FARBER CANCER INSTITUTE · PI DEPINHO, RONALD ANTHONY · 2000 to 2004
$2.1M
NCI NIH HHS R01 CA086379NCI NIH HHS R01CA86379
6 · The paper itself

Abstract

The histone code guides many aspects of chromosome biology including the equal distribution of chromosomes during cell division. In the chromatin domains surrounding the centromere, known as pericentric heterochromatin, histone modifications, particularly deacetylation and methylation, appear to be essential for proper chromosome segregation. However, the specific factors and their precise roles in this highly orchestrated process remain under active investigation. Here, we report that germ-line or somatic deletion of mSds3, an essential component of the functional mSin3/HDAC corepressor complex, generates a cell-lethal condition associated with rampant aneuploidy, defective karyokinesis, and consequently, a failure of cytokinesis. mSds3-deficient cells fail to deacetylate and methylate pericentric heterochromatin histones and to recruit essential heterochromatin-associated proteins, resulting in aberrant associations among heterologous chromosomes via centromeric regions and consequent failure to properly segregate chromosomes. Mutant mSds3 molecules that are defective in mSin3 binding fail to rescue the mSds3 null phenotypes. On the basis of these findings, we propose that mSds3 and its associated mSin3/HDAC components play a central role in initiating the cascade of pericentric heterochromatin-specific modifications necessary for the proper distribution of chromosomes during cell division in mammalian cells.

Indexed as

Chromosome SegregationRepressor ProteinsAcetylationAneuploidyAnimalsBlastocystCarboxylic Ester HydrolasesCells, CulturedFibroblastsGene Expression Regulation, DevelopmentalHeterochromatinHistone DeacetylasesHistonesIntegrasesMammalsMethylationCarboxylic Ester HydrolasesCre recombinaseHeterochromatinHistone DeacetylasesHistonesIntegrasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSDS3 protein, S cerevisiaeSIN3 protein, S cerevisiaeTranscription FactorsViral Proteins

Identifiers

PMID14522945
PMCPMC218077
OpenAlexW2156719499

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.