Evidence map›Paper›PMID 28733645›Full record

ArticleNature communications2017

HDAC3 is a molecular brake of the metabolic switch supporting white adipose tissue browning.

Alessandra Ferrari, Raffaella Longo, Erika Fiorino, Rui Silva, Nico Mitro, Gaia Cermenati, Federica Gilardi, Béatrice Desvergne, Annapaola Andolfo, Cinzia Magagnotti and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 84 citations in OpenAlex.

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  6. Maintenance of thermogenic adipose tissues despite loss of the H3K27 acetyltransferases p300 or CBP.American journal of physiology. Endocrinology and metabolism · 2024
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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

14 authors at 4 institutions in 3 countries.

Alessandra FerrariDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.ORCID http://orcid.org/0000-0001-7354-9895
Raffaella LongoDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Erika FiorinoDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Rui SilvaDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Nico MitroDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.ORCID http://orcid.org/0000-0002-5000-3619
Gaia CermenatiDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Federica GilardiCentre Intégratif de Génomique, Université de Lausanne, Lausanne, 1015, Switzerland.
Béatrice DesvergneCentre Intégratif de Génomique, Université de Lausanne, Lausanne, 1015, Switzerland.
Annapaola AndolfoProMiFa, Protein Microsequencing Facility, San Raffaele Scientific Institute, Milano, 20132, Italy.
Cinzia MagagnottiProMiFa, Protein Microsequencing Facility, San Raffaele Scientific Institute, Milano, 20132, Italy.ORCID http://orcid.org/0000-0001-9077-2757
Donatella CarusoDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Emma De FabianiDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy.
Scott W HiebertDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Maurizio CrestaniDipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milano, 20133, Italy. maurizio.crestani@unimi.it.ORCID http://orcid.org/0000-0001-9230-1078
University of Milan · ITUniversity of Lausanne · CHUniversity of California, Los Angeles · USVanderbilt University · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
NIDDK NIH HHS P30 DK058404
6 · The paper itself

Abstract

White adipose tissue (WAT) can undergo a phenotypic switch, known as browning, in response to environmental stimuli such as cold. Post-translational modifications of histones have been shown to regulate cellular energy metabolism, but their role in white adipose tissue physiology remains incompletely understood. Here we show that histone deacetylase 3 (HDAC3) regulates WAT metabolism and function. Selective ablation of Hdac3 in fat switches the metabolic signature of WAT by activating a futile cycle of de novo fatty acid synthesis and β-oxidation that potentiates WAT oxidative capacity and ultimately supports browning. Specific ablation of Hdac3 in adipose tissue increases acetylation of enhancers in Pparg and Ucp1 genes, and of putative regulatory regions of the Ppara gene. Our results unveil HDAC3 as a regulator of WAT physiology, which acts as a molecular brake that inhibits fatty acid metabolism and WAT browning.Histone deacetylases, such as HDAC3, have been shown to alter cellular metabolism in various tissues. Here the authors show that HDAC3 regulates WAT metabolism by activating a futile cycle of fatty acid synthesis and oxidation, which supports WAT browning.

Indexed as

AdipocytesAdipose Tissue, BrownAdipose Tissue, WhiteAnimalsCell LineDiet, High-FatGene Expression RegulationGene SilencingHistone Deacetylase 3Histone DeacetylasesLipid MetabolismMaleMiceMice, KnockoutHistone Deacetylase 3Histone Deacetylases

Identifiers

PMID28733645
PMCPMC5522415
OpenAlexW2735085565

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.