Mechanisms and Dynamics of Protein Acetylation in Mitochondria

被引:235
|
作者
Baeza, Josue [1 ,2 ]
Smallegan, Michael J. [2 ]
Denu, John M. [1 ,2 ]
机构
[1] Univ Wisconsin, Dept Biomol Chem, Madison, WI 53715 USA
[2] Univ Wisconsin, Wisconsin Inst Discovery, Madison, WI 53715 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
BOVINE GLUTAMATE-DEHYDROGENASE; FATTY-ACID OXIDATION; LYSINE ACETYLATION; SIRT3; DEACETYLATES; HISTONE ACETYLTRANSFERASE; DEPENDENT REGULATION; CALORIE RESTRICTION; COA SYNTHETASE; HEXOKINASE II; CYCLOPHILIN D;
D O I
10.1016/j.tibs.2015.12.006
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
Reversible protein acetylation is a major regulatory mechanism for controlling protein function. Through genetic manipulations, dietary perturbations, and new proteomic technologies, the diverse functions of protein acetylation are coming into focus. Protein acetylation in mitochondria has taken center stage, revealing that 63% of mitochondrially localized proteins contain lysine acetylation sites. We summarize the field and discuss salient topics that cover spurious versus targeted acetylation, the role of SIRT3 deacetylation, nonenzymatic acetylation, and molecular models for regulatory acetylations that display high and low stoichiometry.
引用
收藏
页码:231 / 244
页数:14
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