Evidence map›Paper›PMID 25501812›Full record

ArticleJournal of cell science2015

The NuRD nucleosome remodelling complex and NHK-1 kinase are required for chromosome condensation in oocytes.

Elvira Nikalayevich, Hiroyuki Ohkura

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
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  7. Epigenetic regulation of post-embryonic development.Current opinion in insect science · 2021
    Review
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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

2 authors at 1 institution in 1 country.

Elvira Nikalayevich
Hiroyuki Ohkura
University of Edinburgh · GB

Funding

Drosophila Transgenic RNAi Resource ProjectR01GM084947 · NIGMS · HARVARD MEDICAL SCHOOL · PI PERRIMON, NORBERT · 2008 to 2019
$9.8M
NIGMS NIH HHS R01 GM084947NIGMS NIH HHS R01-GM084947Wellcome Trust 98030
6 · The paper itself

Abstract

Chromosome condensation during cell division is one of the most dramatic events in the cell cycle. Condensin and topoisomerase II are the most studied factors in chromosome condensation. However, their inactivation leads to only mild defects and little is known about the roles of other factors. Here, we took advantage of Drosophilaoocytes to elucidate the roles of potential condensation factors by performing RNA interference (RNAi). Consistent with previous studies, depletion of condensin I subunits or topoisomerase II in oocytes only mildly affected chromosome condensation. In contrast, we found severe undercondensation of chromosomes after depletion of the Mi-2-containing NuRD nucleosome remodelling complex or the protein kinase NHK-1 (also known as Ballchen in Drosophila). The further phenotypic analysis suggests that Mi-2 and NHK-1 are involved in different pathways of chromosome condensation. We show that the main role of NHK-1 in chromosome condensation is to phosphorylate Barrier-to-autointegration factor (BAF) and suppress its activity in linking chromosomes to nuclear envelope proteins. We further show that NHK-1 is important for chromosome condensation during mitosis as well as in oocytes.

Indexed as

Adenosine TriphosphatasesAnimalsCell Cycle ProteinsChromosomesDNA-Binding ProteinsDNA Topoisomerases, Type IIDrosophila melanogasterDrosophila ProteinsMi-2 Nucleosome Remodeling and Deacetylase ComplexMitosisMultiprotein ComplexesNuclear EnvelopeNuclear ProteinsOocytesPhosphorylationProtamine KinaseAdenosine TriphosphatasesBAF protein, DrosophilaBall protein, DrosophilaCell Cycle Proteinscondensin complexesDNA-Binding ProteinsDNA Topoisomerases, Type IIDrosophila ProteinsMi-2 Nucleosome Remodeling and Deacetylase ComplexMultiprotein ComplexesNuclear ProteinsProtamine KinaseRNA, Small Interfering

Identifiers

PMID25501812
PMCPMC4311133
OpenAlexW2163065064

What OpenQuestion holds

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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.