A Molecular Perspective on Sirtuin Activity

• Type: Article in International Scientific Journal
• Date: 2020

Authors

Teixeira, CSS (Author) Other; Nuno M F S A Cerqueira (Author) FCUP; Pedro Gomes (Author) FMUP; Sergio Filipe Sousa (Author) FCUP

Journal

Title: International Journal Of Molecular Sciences

Vol. 21 No. 7

Pages: 1-20

ISSN: 1661-6596

Publisher: MDPI

Indexing

ISI Web of Knowledge - 16 Citations

Scopus - 15 Citations

Other information

Authenticus ID: P-00T-1JH

DOI: 10.3390/ijms21228609

Abstract (EN): The protein acetylation of either the alpha-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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 20