Huang Jing-Yi, Hirschey Matthew D, Shimazu Tadahiro, Ho Linh, Verdin Eric
Gladstone Institute of Virology and Immunology, University of California, San Francisco, CA, USA.
Biochim Biophys Acta. 2010 Aug;1804(8):1645-51. doi: 10.1016/j.bbapap.2009.12.021. Epub 2010 Jan 7.
Sirtuins have emerged as important proteins in aging, stress resistance and metabolic regulation. Three sirtuins, SIRT3, 4 and 5, are located within the mitochondrial matrix. SIRT3 and SIRT5 are NAD(+)-dependent deacetylases that remove acetyl groups from acetyllysine-modified proteins and yield 2'-O-acetyl-ADP-ribose and nicotinamide. SIRT4 can transfer the ADP-ribose group from NAD(+) onto acceptor proteins. Recent findings reveal that a large fraction of mitochondrial proteins are acetylated and that mitochondrial protein acetylation is modulated by nutritional status. This and the identification of targets for SIRT3, 4 and 5 support the model that mitochondrial sirtuins are metabolic sensors that modulate the activity of metabolic enzymes via protein deacetylation or mono-ADP-ribosylation. Here, we review and discuss recent progress in the study of mitochondrial sirtuins and their targets.
沉默调节蛋白已成为衰老、抗逆性和代谢调节方面的重要蛋白质。三种沉默调节蛋白,即SIRT3、SIRT4和SIRT5,位于线粒体基质中。SIRT3和SIRT5是依赖烟酰胺腺嘌呤二核苷酸(NAD(+))的去乙酰化酶,可从乙酰赖氨酸修饰的蛋白质上去除乙酰基,并生成2'-O-乙酰-ADP-核糖和烟酰胺。SIRT4可将NAD(+)上的ADP-核糖基团转移到受体蛋白上。最近的研究结果表明,很大一部分线粒体蛋白质会发生乙酰化,且线粒体蛋白质乙酰化受营养状况的调节。这一点以及对SIRT3、SIRT4和SIRT5靶点的鉴定支持了这样一种模型,即线粒体沉默调节蛋白是代谢传感器,可通过蛋白质去乙酰化或单ADP-核糖基化来调节代谢酶的活性。在此,我们综述并讨论线粒体沉默调节蛋白及其靶点研究的最新进展。