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The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging

Protein N-ε-lysine acetylation is is an important post-translational modification that plays critical roles in the regulation of many cellular processes. A role for this modification in the process of aging goes back two decades to the discovery that the yeast NAD(+)-dependent histone deacetylase Si...

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Autores principales: Nagarajan, Prabakaran, Parthun, Mark R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7093178/
https://www.ncbi.nlm.nih.gov/pubmed/32170047
http://dx.doi.org/10.18632/aging.102949
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author Nagarajan, Prabakaran
Parthun, Mark R.
author_facet Nagarajan, Prabakaran
Parthun, Mark R.
author_sort Nagarajan, Prabakaran
collection PubMed
description Protein N-ε-lysine acetylation is is an important post-translational modification that plays critical roles in the regulation of many cellular processes. A role for this modification in the process of aging goes back two decades to the discovery that the yeast NAD(+)-dependent histone deacetylase Sir2 regulates lifespan in yeast. While the Sirtuin family of protein deacetylases has been intensively studied in many model systems and is definitively linked to aging, the enzymes responsible for protein acetylation, protein acetyltransferases (KATs), have not received a similar level of attention. However, a series of recent studies have directly explored the role of specific KATs in aging. These studies have shown that modulation of KAT activity can influence cellular pathways important for aging and directly effect organismal lifespan.
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spelling pubmed-70931782020-03-30 The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging Nagarajan, Prabakaran Parthun, Mark R. Aging (Albany NY) Research Perspective Protein N-ε-lysine acetylation is is an important post-translational modification that plays critical roles in the regulation of many cellular processes. A role for this modification in the process of aging goes back two decades to the discovery that the yeast NAD(+)-dependent histone deacetylase Sir2 regulates lifespan in yeast. While the Sirtuin family of protein deacetylases has been intensively studied in many model systems and is definitively linked to aging, the enzymes responsible for protein acetylation, protein acetyltransferases (KATs), have not received a similar level of attention. However, a series of recent studies have directly explored the role of specific KATs in aging. These studies have shown that modulation of KAT activity can influence cellular pathways important for aging and directly effect organismal lifespan. Impact Journals 2020-03-13 /pmc/articles/PMC7093178/ /pubmed/32170047 http://dx.doi.org/10.18632/aging.102949 Text en Copyright © 2020 Nagarajan and Parthun. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Perspective
Nagarajan, Prabakaran
Parthun, Mark R.
The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title_full The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title_fullStr The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title_full_unstemmed The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title_short The flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
title_sort flip side of sirtuins: the emerging roles of protein acetyltransferases in aging
topic Research Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7093178/
https://www.ncbi.nlm.nih.gov/pubmed/32170047
http://dx.doi.org/10.18632/aging.102949
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