Evidence map›Paper›PMID 22375075›Full record

ArticleMolecular & cellular proteomics : MCP2012

Estrogen receptor alpha interacts with mitochondrial protein HADHB and affects beta-oxidation activity.

Zhenqi Zhou, Jianhong Zhou, Yuchun Du

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed, 60 citations in OpenAlex.

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  17. A long noncoding RNA regulates inflammation resolution by mouse macrophages through fatty acid oxidation activation.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

3 authors at 1 institution in 1 country.

Zhenqi ZhouDepartment of Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701, USA.
Jianhong Zhou
Yuchun Du
University of Arkansas at Fayetteville · US

Funding

Center for Protein Structure and FunctionP30GM103450 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2012 to 2014
$3.2M
RESEARCH PILOT PROJECT PROGRAMP30RR031154 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI HINTON, JAMES F · 2010 to 2011
$2.2M
NCRR NIH HHS 5P30RR031154NCRR NIH HHS P30 RR031154NIGMS NIH HHS P30 GM103450
6 · The paper itself

Abstract

It is known that estrogen receptors can function as nuclear receptors and transcription factors in the nucleus and as signaling molecules in the plasma membrane. In addition, the localization of the receptors in mitochondria suggests that they may play important roles in mitochondria. In order to identify novel proteins that are involved in ERα-mediated actions of estrogens, we used a proteomic method that integrated affinity purification, two-dimensional gel electrophoresis, and mass spectrometry to isolate and identify cellular proteins that interact with ERα. One of the proteins identified was trifunctional protein β-subunit (HADHB), a mitochondrial protein that is required for β-oxidation of fatty acids in mitochondria. We have verified the interaction between ERα and HADHB by coimmunoprecipitation and established that ERα directly binds to HADHB by performing an in vitro binding assay. In addition, we have shown that ERα colocalizes with HADHB in the mitochondria by confocal microscopy, and the two proteins interact with each other within mitochondria by performing coimmunoprecipitation using purified mitochondria as starting materials. We have demonstrated that the expression of ERα affects HADHB activity, and a combination of 17β-estrodiol and tamoxifen affects the activity of HADHB prepared from human breast cancer cells that express ERα but not from the cells that are ERα deficient. Furthermore, we have demonstrated that 17β-estrodiol plus tamoxifen affects the association of ERα with HADHB in human cell extract. Our results suggest that HADHB is a functional molecular target of ERα in the mitochondria, and the interaction may play an important role in the estrogen-mediated lipid metabolism in animals and humans.

Indexed as

Binding SitesCell Line, TumorCell MembraneElectrophoresis, Gel, Two-DimensionalEscherichia coliEstradiolEstrogen Receptor alphaFemaleGene ExpressionHumansImmunoprecipitationLipid MetabolismMicroscopy, ConfocalMitochondriaMitochondrial Trifunctional ProteinMitochondrial Trifunctional Protein, beta SubunitESR1 protein, humanEstradiolEstrogen Receptor alphaHADHB protein, humanMitochondrial Trifunctional ProteinMitochondrial Trifunctional Protein, beta SubunitMultienzyme ComplexesTamoxifen

Identifiers

PMID22375075
PMCPMC3394935
OpenAlexW2136707042

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.