Protein acetylation in metabolism — metabolites and cofactors

Keir J. Menzies; Hongbo Zhang; Elena Katsyuba; Johan Auwerx

doi:10.1038/nrendo.2015.181

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Publisher: Springer Journals
Copyright: Copyright © 2015 by Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
Subject: Medicine & Public Health; Medicine/Public Health, general; Endocrinology
ISSN: 1759-5029
eISSN: 1759-5037
DOI: 10.1038/nrendo.2015.181
Publisher site: See Article on Publisher Site

Abstract

Acetylation is a key post-translational modification that integrates metabolic flux and physiological processes within cells, including circadian rhythm, cell cycle and energy production Lysine acetyltransferases (KATs) and lysine deacetylases (KDACs) are responsible for reversible changes in protein acetylation status Metabolites or cofactors, including nicotinamide adenine dinucleotide (NAD+), nicotinamide, coenzyme A, acetyl coenzyme A, zinc and butyrate and/or β-hydroxybutyrate, directly alter KAT or KDAC activity to link energy status with cellular and organismal homeostasis The association between NAD+ and sirtuin-mediated mitochondrial improvements is clinically relevant, but the translational potential between other metabolites and cofactors and acetylation and/or deactylation reactions is less clear

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Nature Reviews Endocrinology – Springer Journals

Published: Oct 27, 2015

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Protein acetylation in metabolism — metabolites and cofactors

Protein acetylation in metabolism — metabolites and cofactors

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Protein acetylation in metabolism — metabolites and cofactors

Protein acetylation in metabolism — metabolites and cofactors

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