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The world of protein acetylation
被引:565
|作者:
Drazic, Adrian
[1
]
Myklebust, Line M.
[1
]
Ree, Rasmus
[1
,2
]
Arnesen, Thomas
[1
,2
]
机构:
[1] Univ Bergen, Dept Mol Biol, Thormohlensgate 55, N-5020 Bergen, Norway
[2] Haukeland Hosp, Dept Surg, N-5021 Bergen, Norway
来源:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
|
2016年
/
1864卷
/
10期
关键词:
Post-translational modification;
lysine acetylation;
N-terminal acetylation;
acetyltransferase;
deacetylation;
KAT;
NAT;
HAT;
N-TERMINAL ACETYLATION;
RUBINSTEIN-TAYBI-SYNDROME;
HISTONE DEACETYLASE EXPRESSION;
CONTROLS CHONDROCYTE HYPERTROPHY;
ALPHA-ACETYLTRANSFERASE NATA;
FATTY-ACID OXIDATION;
EXTENDS LIFE-SPAN;
DE-NOVO MUTATIONS;
CELL LUNG-CANCER;
LYSINE-ACETYLATION;
D O I:
10.1016/j.bbapap.2016.06.007
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl coenzyme A, can be co- or post-translationally attached to either the alpha-amino group of the N-terminus of proteins or to the c-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation. (C) 2016 The Authors. Published by Elsevier B.V.
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页码:1372 / 1401
页数:30
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