First Things First: Vital Protein Varks by N-Terminal Acetyltransferases

被引:200
作者
Aksnes, Henriette [1 ]
Drazic, Adrian [1 ]
Marie, Michael [1 ]
Arnesen, Thomas [1 ,2 ]
机构
[1] Univ Bergen, Dept Mol Biol, N-5020 Bergen, Norway
[2] Haukeland Hosp, Dept Surg, N-5021 Bergen, Norway
关键词
ALPHA-ACETYLTRANSFERASE; MOLECULAR-BASIS; INTELLECTUAL DISABILITY; CELLULAR-PROTEINS; CRYSTAL-STRUCTURE; SIR3; STABILIZES; GTPASE ARL3P; ACETYLATION; IDENTIFICATION; YEAST;
D O I
10.1016/j.tibs.2016.07.005
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
N-terminal (Nt) acetylation is known to be a highly abundant co-translational protein modification, but the recent discovery of Golgi- and chloroplast-resident N-terminal acetyltransferases (NATs) revealed that it can also be added post-translationally. Nt-acetylation may act as a degradation signal in a novel branch of the N-end rule pathway, whose functions include the regulation of human blood pressure. Nt-acetylation also modulates protein interactions, targeting, and folding. In plants, Nt-acetylation plays a role in the control of resistance to drought and in regulation of immune responses. Mutations of specific human NATs that decrease their activity can cause either the lethal Ogden syndrome or severe intellectual disability and cardiovascular defects. In sum, recent advances highlight Nt-acetylation as a key factor in many biological pathways.
引用
收藏
页码:746 / 760
页数:15
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