Evidence map›Paper›PMID 20400511›Full record

ArticleThe Journal of biological chemistry2010

Double PHD fingers protein DPF2 recognizes acetylated histones and suppresses the function of estrogen-related receptor alpha through histone deacetylase 1.

Reiko Matsuyama, Ichiro Takada, Atsushi Yokoyama, Sally Fujiyma-Nakamura, Naoya Tsuji, Hirochika Kitagawa, Ryoji Fujiki, Misun Kim, Madoka Kouzu-Fujita, Tetsu Yano and 1 more

RetractedOpen access · hybridAbstract readRetracted Publication
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Reiko MatsuyamaInstitute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.
Ichiro Takada
Atsushi Yokoyama
Sally Fujiyma-Nakamura
Naoya Tsuji
Hirochika Kitagawa
Ryoji Fujiki
Misun Kim
Madoka Kouzu-Fujita
Tetsu Yano
Shigeaki Kato
The University of Tokyo · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Estrogen-related receptor alpha (ERRalpha) is a member of the nuclear receptor superfamily and regulates many physiological functions, including mitochondrial biogenesis and lipid metabolism. ERRalpha enhances the transactivation function without endogenous ligand by associating with coactivators such as peroxisome proliferator-activated receptor gamma coactivator 1 alpha and beta (PGC-1alpha and -beta) and members of the steroid receptor coactivator family. However, the molecular mechanism by which the transactivation function of ERRalpha is converted from a repressive state to an active state is poorly understood. Here we used biochemical purification techniques to identify ERRalpha-associated proteins in HeLa cells stably expressing ERRalpha. Interestingly, we found that double PHD fingers protein DPF2/BAF45d suppressed PGC-1alpha-dependent transactivation of ERRalpha by recognizing acetylated histone H3 and associating with HDAC1. DPF2 directly bound to ERRalpha and suppressed the transactivation function of nuclear receptors such as androgen receptor. DPF2 was recruited to ERR target gene promoters in myoblast cells, and knockdown of DPF2 derepressed the level of mRNA expressed by target genes of ERRalpha. These results show that DPF2 acts as a nuclear receptor-selective co-repressor for ERRalpha by associating with both acetylated histone H3 and HDAC1.

Indexed as

AcetylationAnimalsCell DifferentiationCell NucleusDNA-Binding ProteinsERRalpha Estrogen-Related ReceptorHistone Deacetylase 1HistonesHumansMiceMutationProtein Structure, TertiaryReceptors, EstrogenRepressor ProteinsRNA, MessengerTranscriptional ActivationDNA-Binding ProteinsDPF2 protein, humanDPF2 protein, mouseERRalpha Estrogen-Related ReceptorHistone Deacetylase 1HistonesReceptors, EstrogenRepressor ProteinsRNA, MessengerTranscription Factors

Identifiers

PMID20400511
PMCPMC2881740
OpenAlexW2056711185

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.