Protein Lysine Acetylation: Grease or Sand in the Gears of β-Cell Mitochondria?

被引:7
|
作者
Santo-Domingo, Jaime [1 ]
Dayon, Loiec [2 ]
Wiederkehr, Andreas [1 ]
机构
[1] Nestle Inst Hlth Sci, Mitochondrial Funct, CH-1015 Lausanne, Switzerland
[2] Nestle Inst Hlth Sci, Prote, CH-1015 Lausanne, Switzerland
关键词
STIMULATED INSULIN-SECRETION; GLUCOSE-REGULATED ANAPLEROSIS; SKELETAL-MUSCLE MITOCHONDRIA; FATTY-ACID OXIDATION; PANCREATIC-ISLETS; ATP SYNTHASE; NICOTINAMIDE MONONUCLEOTIDE; DIABETES-MELLITUS; ENERGY-METABOLISM; SIRT3; DEFICIENCY;
D O I
10.1016/j.jmb.2019.09.011
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
Mitochondria carry out many essential functions in metabolism. A central task is the oxidation of nutrients and the generation of ATP by oxidative phosphorylation. Mitochondrial metabolism needs to be tightly regulated for the cell to respond to changes in ATP demand and nutrient supply. Here, we review how protein lysine acetylation contributes to the regulation of mitochondrial metabolism in insulin target tissues and the insulin-secreting pancreatic beta-cell. We summarize recent evidence showing that in pancreatic beta-cells, lysine acetylation occurs on a large number of proteins involved in metabolism. Furthermore, we give a brief overview of the molecular mechanism that controls lysine acetylation dynamics. We propose that protein lysine acetylation is an important mechanism for the fine-tuning of mitochondrial activity in beta-cells during normal physiology. In contrast, nutrient oversupply, oxidative stress, or inhibition of the mitochondrial deacetylase SIRT3 leads to protein lysine hyperacetylation, which impairs mitochondrial function. By perturbing mitochondrial activity in beta-cells and insulin target tissues, protein lysine hyperacetylation may contribute to the development of type 2 diabetes. (C) 2019 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1446 / 1460
页数:15
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