Evidence map›Paper›PMID 23612983›Full record

ArticleThe Journal of biological chemistry2013

Protein kinase CK2 regulates the dimerization of histone deacetylase 1 (HDAC1) and HDAC2 during mitosis.

Dilshad H Khan, Shihua He, Jenny Yu, Stefan Winter, Wenguang Cao, Christian Seiser, James R Davie

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

41 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. CK2B Induces CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    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

7 authors at 5 institutions in 3 countries.

Dilshad H KhanManitoba Institute of Child Health, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada.
Shihua HeManitoba Institute of Child Health, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada.
Jenny YuMelanoma Medical Oncology, M.D. Anderson Cancer Center, Houston, Texas 77054.
Stefan WinterMax F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria.
Wenguang CaoManitoba Institute of Child Health, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada.
Christian SeiserMax F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria.
James R DavieManitoba Institute of Child Health, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada. Electronic address: davie@cc.umanitoba.ca.
Children's Hospital Research Institute of Manitoba · CAMedical University of Vienna · ATThe University of Texas MD Anderson Cancer Center · USUniversity of Manitoba · CAVienna Biocenter · AT

Funding

Canadian Institutes of Health Research MOP-9186
6 · The paper itself

Abstract

Histone deacetylase 1 (HDAC1) and HDAC2 are components of corepressor complexes that are involved in chromatin remodeling and regulation of gene expression by regulating dynamic protein acetylation. HDAC1 and -2 form homo- and heterodimers, and their activity is dependent upon dimer formation. Phosphorylation of HDAC1 and/or HDAC2 in interphase cells is required for the formation of HDAC corepressor complexes. In this study, we show that during mitosis, HDAC2 and, to a lesser extent, HDAC1 phosphorylation levels dramatically increase. When HDAC1 and -2 are displaced from the chromosome during metaphase, they dissociate from each other, but each enzyme remains in association with components of the HDAC corepressor complexes Sin3, NuRD, and CoREST as homodimers. Enzyme inhibition studies and mutational analyses demonstrated that protein kinase CK2-catalyzed phosphorylation of HDAC1 and -2 is crucial for the dissociation of these two enzymes. These results suggest that corepressor complexes, including HDAC1 or HDAC2 homodimers, might target different cellular proteins during mitosis.

Indexed as

Casein Kinase IChromosomes, HumanCo-Repressor ProteinsHEK293 CellsHeLa CellsHistone Deacetylase 1Histone Deacetylase 2HumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMitosisMutationNerve Tissue ProteinsPhosphorylationProtein MultimerizationRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexCasein Kinase ICo-Repressor ProteinsHDAC1 protein, humanHDAC2 protein, humanHistone Deacetylase 1Histone Deacetylase 2Mi-2 Nucleosome Remodeling and Deacetylase ComplexNerve Tissue ProteinsRCOR1 protein, humanRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexCorepressor TranscriptionHDAC2 PhosphorylationHistone DeacetylaseMitosisProtein Kinase CK2Protein KinasesProtein Phosphorylation

Identifiers

PMID23612983
PMCPMC3675587
OpenAlexW2042232241

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.