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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/22/8609 |
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| author | Carla S. S. Teixeira Nuno M. F. S. A. Cerqueira Pedro Gomes Sérgio F. Sousa |
| author_facet | Carla S. S. Teixeira Nuno M. F. S. A. Cerqueira Pedro Gomes Sérgio F. Sousa |
| author_sort | Carla S. S. Teixeira |
| collection | DOAJ |
| 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<sup>+</sup> 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. |
| first_indexed | 2024-03-10T14:50:56Z |
| format | Article |
| id | doaj.art-85e4e89470d040b796266b10adfb9109 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T14:50:56Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-85e4e89470d040b796266b10adfb91092023-11-20T21:01:51ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012122860910.3390/ijms21228609A Molecular Perspective on Sirtuin ActivityCarla S. S. Teixeira0Nuno M. F. S. A. Cerqueira1Pedro Gomes2Sérgio F. Sousa3UCIBIO/REQUIMTE, BioSIM - Department of Biomedicine, Faculty of Medicine, University of Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalUCIBIO/REQUIMTE, BioSIM - Department of Biomedicine, Faculty of Medicine, University of Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalDepartment of Biomedicine, Faculty of Medicine, University of Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalUCIBIO/REQUIMTE, BioSIM - Department of Biomedicine, Faculty of Medicine, University of Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalThe 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<sup>+</sup> 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.https://www.mdpi.com/1422-0067/21/22/8609posttranslational modificationsprotein acylationlysine deacetylasessirtuins |
| spellingShingle | Carla S. S. Teixeira Nuno M. F. S. A. Cerqueira Pedro Gomes Sérgio F. Sousa A Molecular Perspective on Sirtuin Activity International Journal of Molecular Sciences posttranslational modifications protein acylation lysine deacetylases sirtuins |
| 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 | posttranslational modifications protein acylation lysine deacetylases sirtuins |
| url | https://www.mdpi.com/1422-0067/21/22/8609 |
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