Center for Molecular Medicine, NHLBI, NIH, Bethesda, MD 20892-1454, USA.
J Mol Cell Cardiol. 2012 Mar;52(3):520-5. doi: 10.1016/j.yjmcc.2011.11.004. Epub 2011 Nov 19.
Although acetyl-modification of protein lysine residues has been recognized for many decades, the appreciation that this post-translational modification is highly prevalent in mitochondria and plays a pivotal regulatory role in mitochondrial function has only become apparent since 2006. The classical biological stressors that modulate mitochondrial protein acetylation include alterations in caloric levels and redox signaling and the major enzyme orchestrating deacetylation is the mitochondrial enriched sirtuin SIRT3. Overall the action of SIRT3 modulates mitochondrial homeostasis and SIRT3 target proteins include mediators of energy metabolism and mitochondrial redox stress adaptive program proteins. Given these effects, it is not surprising that the role of SIRT3 has begun to be implicated in cardiac biology. This review gives a brief overview of sirtuin biology and then focuses on the role of the SIRT3 regulatory program in the control of cardiac hypertrophy and aging. This article is part of a Special Section entitled "Post-translational Modification."
尽管蛋白赖氨酸残基的乙酰化修饰已经被认识了几十年，但直到 2006 年，人们才意识到这种翻译后修饰在线粒体中非常普遍，并在调节线粒体功能方面发挥着关键作用。调节线粒体蛋白乙酰化的经典生物应激因素包括热量水平和氧化还原信号的改变，而主要的去乙酰化酶是富含线粒体的 SIRT3。总的来说，SIRT3 的作用调节线粒体的动态平衡，SIRT3 的靶蛋白包括能量代谢的介质和线粒体氧化还原应激适应程序蛋白。鉴于这些影响，SIRT3 在心脏生物学中的作用开始被牵涉到也就不足为奇了。这篇综述简要概述了 Sirtuin 生物学，然后重点介绍了 SIRT3 调节程序在控制心脏肥大和衰老中的作用。本文是“翻译后修饰”特刊的一部分。
