A Molecular Perspective on Sirtuin Activity

• Tipo: Artigo em Revista Científica Internacional
• Data: 2020

Autores

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

Revista

Título: International Journal Of Molecular Sciences

Vol. 21 Nº 7

Páginas: 1-20

ISSN: 1661-6596

Editora: MDPI

Indexação

ISI Web of Knowledge - 16 Citações

Scopus - 15 Citações

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 20