Evidence map›Paper›PMID 18463162›Full record

ArticleMolecular biology of the cell2008

Signal-dependent regulation of transcription by histone deacetylase 7 involves recruitment to promyelocytic leukemia protein nuclear bodies.

Chengzhuo Gao, Xiwen Cheng, Minh Lam, Yu Liu, Qing Liu, Kun-Sang Chang, Hung-Ying Kao

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

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  7. The Role of HDACs as Leukemia Therapy Targets using HDI.International journal of hematology-oncology and stem cell research · 2015
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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 2 institutions in 1 country.

Chengzhuo GaoDepartment of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Xiwen Cheng
Minh Lam
Yu Liu
Qing Liu
Kun-Sang Chang
Hung-Ying Kao
University Hospitals of Cleveland · USThe University of Texas MD Anderson Cancer Center · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI Amar Desai · 1987 to 2026
$142.3M
Regulation of Gene Expression by PMLR01CA099963 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHANG, KUN-SANG · 2003 to 2007
$1.5M
Regulation of histone deacetylase 7 (HDAC7) activityR01DK062985 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI KAO, HUNG-YING · 2003 to 2006
$998k
NCI NIH HHS P30 CA043703NCI NIH HHS P30 CA43703-12NCI NIH HHS R01 CA-099963NCI NIH HHS R01 CA099963NIDDK NIH HHS R01 DK062985NIDDK NIH HHS R01 DK-62985
6 · The paper itself

Abstract

Promyelocytic leukemia protein (PML) nuclear bodies (NBs) are dynamic subnuclear compartments that play roles in several cellular processes, including apoptosis, transcriptional regulation, and DNA repair. Histone deacetylase (HDAC) 7 is a potent corepressor that inhibits transcription by myocyte enhancer factor 2 (MEF2) transcription factors. We show here that endogenous HDAC7 and PML interact and partially colocalize in PML NBs. Tumor necrosis factor (TNF)-alpha treatment recruits HDAC7 to PML NBs and enhances association of HDAC7 with PML in human umbilical vein endothelial cells. Consequently, TNF-alpha promotes dissociation of HDAC7 from MEF2 transcription factors and the promoters of MEF2 target genes such as matrix metalloproteinase (MMP)-10, leading to accumulation of MMP-10 mRNA. Conversely, knockdown of PML enhances the association between HDAC7 and MEF2 and decreases MMP-10 mRNA accumulation. Accordingly, ectopic expression of PML recruits HDAC7 to PML NBs and leads to activation of MEF2 reporter activity. Notably, small interfering RNA knockdown of PML decreases basal and TNF-alpha-induced MMP-10 mRNA accumulation. Our results reveal a novel mechanism by which PML sequesters HDAC7 to relieve repression and up-regulate gene expression.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsApoptosisHeLa CellsHistone DeacetylasesHumansIntranuclear Inclusion BodiesLeukemia, Promyelocytic, AcuteMatrix Metalloproteinase 10MEF2 Transcription FactorsMiceMicroscopy, ConfocalMyogenic Regulatory FactorsProtein Interaction MappingRNA, Small InterferingTumor Necrosis Factor-alphaHDAC7 protein, humanHdac7 protein, mouseHistone DeacetylasesMatrix Metalloproteinase 10MEF2 Transcription FactorsMyogenic Regulatory FactorsRNA, Small InterferingTumor Necrosis Factor-alpha

Identifiers

PMID18463162
PMCPMC2441690
OpenAlexW2165920649

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.