Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Chem Rev
; 118(3): 1216-1252, 2018 02 14.
Article
em En
| MEDLINE
| ID: mdl-29405707
ABSTRACT
Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Histonas
/
Epigenômica
Limite:
Humans
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article