线粒体蛋白乙酰化调节代谢。
Mitochondrial protein acetylation regulates metabolism.
机构信息
Duke University Medical Center, Durham, NC 27704, U.S.A.
出版信息
Essays Biochem. 2012;52:23-35. doi: 10.1042/bse0520023.
Abstract
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.
摘要
细胞营养物质可用性或能量状态的变化会引起线粒体蛋白乙酰化的全局变化。线粒体中超过三分之一的蛋白质被乙酰化，其中大多数与能量代谢的某个方面有关。线粒体蛋白乙酰化受 SIRT3（sirtuin 3）调节，SIRT3 是 NAD+-依赖性蛋白去乙酰酶家族的成员，最近被确定为能量稳态的关键调节剂。在没有 SIRT3 的情况下，线粒体蛋白过度乙酰化，功能改变，并导致线粒体功能障碍。本章介绍了线粒体蛋白乙酰化的功能影响及其受 SIRT3 调节的综述。
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