Evidence map›Paper›PMID 36861403›Full record

ArticleJournal of cell science2023

Characterization of the nuclear import of the human CHD4-NuRD complex.

Helen Hoffmeister, Simon Holzinger, Marie-Sofie Dürr, Astrid Bruckmann, Susanne Schindler, Regina Gröbner-Ferreira, Reinhard Depping, Gernot Längst

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 2 institutions in 1 country.

Helen HoffmeisterInstitute for Biochemistry, Genetics and Microbiology (Biochemistry III), University of Regensburg, 93053 Regensburg, Germany.
Simon HolzingerInstitute for Biochemistry, Genetics and Microbiology (Biochemistry III), University of Regensburg, 93053 Regensburg, Germany.
Marie-Sofie DürrInstitute for Biochemistry, Genetics and Microbiology (Biochemistry III), University of Regensburg, 93053 Regensburg, Germany.
Astrid BruckmannInstitute for Biochemistry, Genetics and Microbiology (Biochemistry I), University of Regensburg, 93053 Regensburg, Germany.
Susanne SchindlerInstitute of Physiology, AG Hypoxia, University of Lübeck, 23562 Lübeck, Germany.
Regina Gröbner-FerreiraInstitute for Biochemistry, Genetics and Microbiology (Biochemistry III), University of Regensburg, 93053 Regensburg, Germany.
Reinhard DeppingInstitute of Physiology, AG Hypoxia, University of Lübeck, 23562 Lübeck, Germany.
Gernot LängstInstitute for Biochemistry, Genetics and Microbiology (Biochemistry III), University of Regensburg, 93053 Regensburg, Germany.ORCID 0000-0002-8232-1179
University of Regensburg · DEUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin remodeling enzymes form large multiprotein complexes that play central roles in regulating access to the genome. Here, we characterize the nuclear import of the human CHD4 protein. We show that CHD4 enters the nucleus by means of several importin-α proteins (1, 5, 6 and 7), but independently of importin β1. Importin α1 directly interacts with a monopartite 'KRKR'-motif in the N-terminus of CHD4 (amino acids 304-307). However, alanine mutagenesis of this motif only leads to an ∼50% reduction in nuclear localization of CHD4, implying that there are additional import mechanisms. Interestingly, we could show that CHD4 was already associated with the nucleosome remodeling deacetylase (NuRD) core subunits, such as MTA2, HDAC1 and RbAp46 (also known as RBBP7), in the cytoplasm, suggesting an assembly of the NuRD core complex before nuclear import. We propose that, in addition to the importin-α-dependent nuclear localization signal, CHD4 is dragged into the nucleus by a 'piggyback' mechanism using the import signals of the associated NuRD subunits.

Indexed as

Mi-2 Nucleosome Remodeling and Deacetylase ComplexNucleosomesActive Transport, Cell Nucleusalpha KaryopherinsCell NucleusHistone DeacetylasesHumansRepressor Proteinsalpha KaryopherinsCHD4 protein, humanHistone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexMTA2 protein, humanNucleosomesRepressor ProteinsChromatin remodelingNuclear importNuRD

Identifiers

PMID36861403
PMCPMC10112965
OpenAlexW4322757165

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Registered trials

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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.