Modulation of cellular processes by histone and non-histone protein acetylation.
Nat Rev Mol Cell Biol
; 23(5): 329-349, 2022 05.
Article
em En
| MEDLINE
| ID: mdl-35042977
ABSTRACT
Lysine acetylation is a widespread and versatile protein post-translational modification. Lysine acetyltransferases and lysine deacetylases catalyse the addition or removal, respectively, of acetyl groups at both histone and non-histone targets. In this Review, we discuss several features of acetylation and deacetylation, including their diversity of targets, rapid turnover, exquisite sensitivity to the concentrations of the cofactors acetyl-CoA, acyl-CoA and NAD+, and tight interplay with metabolism. Histone acetylation and non-histone protein acetylation influence a myriad of cellular and physiological processes, including transcription, phase separation, autophagy, mitosis, differentiation and neural function. The activity of lysine acetyltransferases and lysine deacetylases can, in turn, be regulated by metabolic states, diet and specific small molecules. Histone acetylation has also recently been shown to mediate cellular memory. These features enable acetylation to integrate the cellular state with transcriptional output and cell-fate decisions.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Histonas
/
Lisina Acetiltransferases
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article