Evidence map›Paper›PMID 20566628›Full record

ArticleThe Journal of biological chemistry2010

Drosophila SIN3 isoforms interact with distinct proteins and have unique biological functions.

Marla M Spain, Joseph A Caruso, Aishwarya Swaminathan, Lori A Pile

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

31 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  4. Heterochromatin-based silencing of a foreign tandem repeat inbioRxiv : the preprint server for biology · 2025
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  16. Review
  17. Crawling wounded: molecular genetic insights into wound healing from Drosophila larvae.The International journal of developmental biology · 2018
    Review
  18. Article
  19. A Looping-Based Model for Quenching Repression.PLoS computational biology · 2017
    Article
  20. 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

4 authors at 1 institution in 1 country.

Marla M SpainDepartment of Biological Sciences, Wayne State University, Detroit, Michigan 48202.
Joseph A CarusoInstitute of Environmental Health Sciences, Wayne State University, Detroit, Michigan 48202.
Aishwarya SwaminathanDepartment of Biological Sciences, Wayne State University, Detroit, Michigan 48202.
Lori A PileDepartment of Biological Sciences, Wayne State University, Detroit, Michigan 48202. Electronic address: loripile@wayne.edu.
Wayne State University · US

Funding

RESEARCH CORE-- SIGNAL TRANSDUCTIONP30ES006639 · NIEHS · WAYNE STATE UNIVERSITY · PI DERESKI, MARY O · 1994 to 2008
$13.1M
NIEHS NIH HHS P30 ES006639NIEHS NIH HHS P30-ES006639
6 · The paper itself

Abstract

The SIN3 corepressor serves as a scaffold for the assembly of histone deacetylase (HDAC) complexes. SIN3 and its associated HDAC have been shown to have critical roles in both development and the regulation of cell cycle progression. Although multiple SIN3 isoforms have been reported in simple to complex eukaryotic organisms, the mechanisms by which such isoforms regulate specific biological processes are still largely uncharacterized. To gain insight into how SIN3 isoform-specific function contributes to the growth and development of a metazoan organism, we have affinity-purified two SIN3 isoform-specific complexes, SIN3 187 and 220, from Drosophila S2 cells and embryos. We have identified a number of proteins common to the complexes, including the HDAC RPD3, as well as orthologs of several proteins known to have roles in regulating cell proliferation in other organisms. We additionally identified factors, including the histone demethylase little imaginal discs and histone-interacting protein p55, that exhibited a preferential interaction with the largest SIN3 isoform. Our experiments indicate that the isoforms are associated with distinct HDAC activity and are recruited to unique and shared sites along polytene chromosome arms. Furthermore, although expression of SIN3 220 can substitute for genetic loss of other isoforms, expression of SIN3 187 does not support Drosophila viability. Together our findings suggest that SIN3 isoforms serve distinct roles in transcriptional regulation by partnering with different histone-modifying enzymes.

Indexed as

AnimalsBody PatterningCell LineCell ProliferationChromosomesDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianHistone Deacetylase 1HistonesMultiprotein ComplexesProtein IsoformsRepressor ProteinsRetinoblastoma-Binding Protein 4Sin3 Histone Deacetylase and Corepressor ComplexTranscription, GeneticCaf1-55 protein, DrosophilaDrosophila ProteinsHDAC1 protein, DrosophilaHistone Deacetylase 1HistonesMultiprotein ComplexesProtein IsoformsRepressor ProteinsRetinoblastoma-Binding Protein 4SIN3A transcription factorSin3 Histone Deacetylase and Corepressor Complex

Identifiers

PMID20566628
PMCPMC2930744
OpenAlexW2158845592

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.