Evidence map›Paper›PMID 22865920›Full record

ArticleMolecular & cellular proteomics : MCP2012

Aurora B-dependent regulation of class IIa histone deacetylases by mitotic nuclear localization signal phosphorylation.

Amanda J Guise, Todd M Greco, Irene Y Zhang, Fang Yu, Ileana M Cristea

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Amanda J GuiseDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Todd M Greco
Irene Y Zhang
Fang Yu
Ileana M Cristea
Princeton University · US

Funding

Proteomic Tools to Uncover the Role of Chromatin Remodeling in HIV-1 InfectionDP1DA026192 · NIDA · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2008 to 2012
$3.9M
NIDA NIH HHS DP1 DA026192NIDA NIH HHS DP1DA026192
6 · The paper itself

Abstract

Class IIa histone deacetylases (HDACs 4/5/7/9) are transcriptional regulators with critical roles in cardiac disease and cancer. HDAC inhibitors are promising anticancer agents, and although they are known to disrupt mitotic progression, the underlying mechanisms of mitotic regulation by HDACs are not fully understood. Here we provide the first identification of histone deacetylases as substrates of Aurora B kinase (AurB). Our study identifies class IIa HDACs as a novel family of AurB targets and provides the first evidence that HDACs are temporally and spatially regulated by phosphorylation during the cell cycle. We define the precise site of AurB-mediated phosphorylation as a conserved serine within the nuclear localization signals of HDAC4, HDAC5, and HDAC9 at Ser265, Ser278, and Ser242, respectively. We establish that AurB interacts with these HDACs in vivo, and that this association increases upon disruption of 14-3-3 binding. We observe colocalization of endogenous, phosphorylated HDACs with AurB at the mitotic midzone in late anaphase and the midbody during cytokinesis, complemented by a reduction in HDAC interactions with components of the nuclear corepressor complex. We propose that AurB-dependent phosphorylation of HDACs induces sequestration within a phosphorylation gradient at the midzone, maintaining separation from re-forming nuclei and contributing to transcriptional control.

Indexed as

MitosisAmino Acid SequenceAurora Kinase BAurora KinasesCell LineChromatography, AffinityConserved SequenceCytokinesisHistone DeacetylasesHumansModels, BiologicalMolecular Sequence DataNuclear Localization SignalsNuclear Receptor Co-Repressor 1PhosphorylationPhosphoserineAURKB protein, humanAurora Kinase BAurora KinasesHistone DeacetylasesNuclear Localization SignalsNuclear Receptor Co-Repressor 1PhosphoserineProtein Serine-Threonine Kinases

Identifiers

PMID22865920
PMCPMC3494195
OpenAlexW2132189181

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.