Cargando…
A Molecular Perspective on Sirtuin Activity
The protein acetylation of either the α-amino groups of amino-terminal residues or of internal lysine or cysteine residues is one of the major posttranslational protein modifications that occur in the cell with repercussions at the protein as well as at the metabolome level. The lysine acetylation s...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7696986/ https://www.ncbi.nlm.nih.gov/pubmed/33203121 http://dx.doi.org/10.3390/ijms21228609 |
_version_ | 1783615530304798720 |
---|---|
author | Teixeira, Carla S. S. Cerqueira, Nuno M. F. S. A. Gomes, Pedro Sousa, Sérgio F. |
author_facet | Teixeira, Carla S. S. Cerqueira, Nuno M. F. S. A. Gomes, Pedro Sousa, Sérgio F. |
author_sort | Teixeira, Carla S. S. |
collection | PubMed |
description | The protein acetylation of either the α-amino groups of amino-terminal residues or of internal lysine or cysteine residues is one of the major posttranslational protein modifications that occur in the cell with repercussions at the protein as well as at the metabolome level. The lysine acetylation status is determined by the opposing activities of lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), which add and remove acetyl groups from proteins, respectively. A special group of KDACs, named sirtuins, that require NAD(+) as a substrate have received particular attention in recent years. They play critical roles in metabolism, and their abnormal activity has been implicated in several diseases. Conversely, the modulation of their activity has been associated with protection from age-related cardiovascular and metabolic diseases and with increased longevity. The benefits of either activating or inhibiting these enzymes have turned sirtuins into attractive therapeutic targets, and considerable effort has been directed toward developing specific sirtuin modulators. This review summarizes the protein acylation/deacylation processes with a special focus on the current developments in the sirtuin research field. |
format | Online Article Text |
id | pubmed-7696986 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76969862020-11-29 A Molecular Perspective on Sirtuin Activity Teixeira, Carla S. S. Cerqueira, Nuno M. F. S. A. Gomes, Pedro Sousa, Sérgio F. Int J Mol Sci Review The protein acetylation of either the α-amino groups of amino-terminal residues or of internal lysine or cysteine residues is one of the major posttranslational protein modifications that occur in the cell with repercussions at the protein as well as at the metabolome level. The lysine acetylation status is determined by the opposing activities of lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), which add and remove acetyl groups from proteins, respectively. A special group of KDACs, named sirtuins, that require NAD(+) as a substrate have received particular attention in recent years. They play critical roles in metabolism, and their abnormal activity has been implicated in several diseases. Conversely, the modulation of their activity has been associated with protection from age-related cardiovascular and metabolic diseases and with increased longevity. The benefits of either activating or inhibiting these enzymes have turned sirtuins into attractive therapeutic targets, and considerable effort has been directed toward developing specific sirtuin modulators. This review summarizes the protein acylation/deacylation processes with a special focus on the current developments in the sirtuin research field. MDPI 2020-11-15 /pmc/articles/PMC7696986/ /pubmed/33203121 http://dx.doi.org/10.3390/ijms21228609 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Teixeira, Carla S. S. Cerqueira, Nuno M. F. S. A. Gomes, Pedro Sousa, Sérgio F. A Molecular Perspective on Sirtuin Activity |
title | A Molecular Perspective on Sirtuin Activity |
title_full | A Molecular Perspective on Sirtuin Activity |
title_fullStr | A Molecular Perspective on Sirtuin Activity |
title_full_unstemmed | A Molecular Perspective on Sirtuin Activity |
title_short | A Molecular Perspective on Sirtuin Activity |
title_sort | molecular perspective on sirtuin activity |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7696986/ https://www.ncbi.nlm.nih.gov/pubmed/33203121 http://dx.doi.org/10.3390/ijms21228609 |
work_keys_str_mv | AT teixeiracarlass amolecularperspectiveonsirtuinactivity AT cerqueiranunomfsa amolecularperspectiveonsirtuinactivity AT gomespedro amolecularperspectiveonsirtuinactivity AT sousasergiof amolecularperspectiveonsirtuinactivity AT teixeiracarlass molecularperspectiveonsirtuinactivity AT cerqueiranunomfsa molecularperspectiveonsirtuinactivity AT gomespedro molecularperspectiveonsirtuinactivity AT sousasergiof molecularperspectiveonsirtuinactivity |