Evidence map›Paper›PMID 18535655›Full record

ArticlePLoS genetics2008

Genetic identification of a network of factors that functionally interact with the nucleosome remodeling ATPase ISWI.

Giosalba Burgio, Gaspare La Rocca, Anna Sala, Walter Arancio, Dario Di Gesù, Marianna Collesano, Adam S Sperling, Jennifer A Armstrong, Simon J van Heeringen, Colin Logie and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Frontiers in epigenetics and epigenomics · 2024
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  5. Elements of the cellular metabolic structure.Frontiers in molecular biosciences · 2015
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  15. Article
  16. The roles of PARP1 in gene control and cell differentiation.Current opinion in genetics & development · 2010
    Review
  17. Article
  18. Article
  19. 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

12 authors at 5 institutions in 3 countries.

Giosalba BurgioDipartimento di Scienze Biochimiche, Universita' degli Studi di Palermo, Palermo, Italy.
Gaspare La Rocca
Anna Sala
Walter Arancio
Dario Di Gesù
Marianna Collesano
Adam S Sperling
Jennifer A Armstrong
Simon J van Heeringen
Colin Logie
John W Tamkun
Davide F V Corona
University of California, Santa Cruz · USDulbecco Telethon Institute · ITUniversity of Palermo · ITRadboud Institute for Molecular Life Sciences · NLRadboud University Medical Center · NL

Funding

Studies of Chromatin Remodeling FactorsR01GM049883 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI TAMKUN, JOHN W. · 1993 to 2013
$3.9M
NIGMS NIH HHS GM49883NIGMS NIH HHS R01 GM049883Telethon TCP03009
6 · The paper itself

Abstract

Nucleosome remodeling and covalent modifications of histones play fundamental roles in chromatin structure and function. However, much remains to be learned about how the action of ATP-dependent chromatin remodeling factors and histone-modifying enzymes is coordinated to modulate chromatin organization and transcription. The evolutionarily conserved ATP-dependent chromatin-remodeling factor ISWI plays essential roles in chromosome organization, DNA replication, and transcription regulation. To gain insight into regulation and mechanism of action of ISWI, we conducted an unbiased genetic screen to identify factors with which it interacts in vivo. We found that ISWI interacts with a network of factors that escaped detection in previous biochemical analyses, including the Sin3A gene. The Sin3A protein and the histone deacetylase Rpd3 are part of a conserved histone deacetylase complex involved in transcriptional repression. ISWI and the Sin3A/Rpd3 complex co-localize at specific chromosome domains. Loss of ISWI activity causes a reduction in the binding of the Sin3A/Rpd3 complex to chromatin. Biochemical analysis showed that the ISWI physically interacts with the histone deacetylase activity of the Sin3A/Rpd3 complex. Consistent with these findings, the acetylation of histone H4 is altered when ISWI activity is perturbed in vivo. These findings suggest that ISWI associates with the Sin3A/Rpd3 complex to support its function in vivo.

Indexed as

AcetylationAdenosine TriphosphatasesAnimalsChromatinChromatin Assembly and DisassemblyChromosomesDrosophila melanogasterDrosophila ProteinsFemaleHistone Deacetylase 1Histone DeacetylasesHistonesMaleNuclear ProteinsNucleosomesProteomicsAdenosine TriphosphatasesChromatinDrosophila ProteinsHDAC1 protein, DrosophilaHistone Deacetylase 1Histone DeacetylasesHistonesISWI proteinNuclear ProteinsNucleosomesRepressor ProteinsSIN3A transcription factorSin3 Histone Deacetylase and Corepressor ComplexTranscription Factors

Identifiers

PMID18535655
PMCPMC2390755
OpenAlexW2014796429

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.