Mitochondrial protein acetylation regulates metabolism.

Mitochondrial protein acetylation regulates metabolism.
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DOI:
10.1042/bse0520023
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发表时间:
2012
影响因子:
6.4
通讯作者:
Hirschey MD
Hirschey MD
中科院分区:
生物学2区
文献类型:
--
作者:
Anderson KA;Hirschey MD

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细胞营养物质利用率或能量状态的变化诱导线粒体蛋白乙酰化的整体变化。线粒体中超过三分之一的蛋白质是乙酰化的,其中大多数参与能量代谢的某些方面。线粒体蛋白乙酰化受SIRT3(sirtuin 3)调节,SIRT3是NAD+依赖性蛋白脱乙酰酶的sirtuin家族的成员,其最近被鉴定为能量稳态的关键调节剂。在缺乏SIRT3的情况下,线粒体蛋白变得高度乙酰化,具有改变的功能,并导致线粒体功能障碍。本章综述了线粒体蛋白乙酰化的功能影响及其SIRT3的调控。
Changes in cellular nutrient availability or energy status induce global changes in mitochondrial protein acetylation. Over one-third of all proteins in the mitochondria are acetylated, of which the majority are involved in some aspect of energy metabolism. Mitochondrial protein acetylation is regulated by SIRT3 (sirtuin 3), a member of the sirtuin family of NAD+-dependent protein deacetylases that has recently been identified as a key modulator of energy homoeostasis. In the absence of SIRT3, mitochondrial proteins become hyperacetylated, have altered function, and contribute to mitochondrial dysfunction. This chapter presents a review of the functional impact of mitochondrial protein acetylation, and its regulation by SIRT3.
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