Laval University Cancer Research Center, Hôtel-Dieu de Québec (CHUQ), 9 McMahon Street, Quebec City, QC, G1R 2J6, Canada.
Cell Mol Life Sci. 2011 Apr;68(7):1147-56. doi: 10.1007/s00018-010-0599-9. Epub 2010 Dec 4.
Covalently modifying a protein has proven to be a powerful mechanism of functional regulation. N-epsilon acetylation of lysine residues was initially discovered on histones and has been studied extensively in the context of chromatin and DNA metabolism, such as transcription, replication and repair. However, recent research shows that acetylation is more widespread than initially thought and that it regulates various nuclear as well as cytoplasmic and mitochondrial processes. In this review, we present the multitude of non-histone proteins targeted by lysine acetyltransferases of the large and conserved MYST family, and known functional consequences of this acetylation. Substrates of MYST enzymes include factors involved in transcription, heterochromatin formation and cell cycle, DNA repair proteins, gluconeogenesis enzymes and finally subunits of MYST protein complexes themselves. Discovering novel substrates of MYST proteins is pivotal for the understanding of the diverse functions of these essential acetyltransferases in nuclear processes, signaling, stress response and metabolism.
共价修饰蛋白质已被证明是一种强大的功能调节机制。赖氨酸残基的 N-ε 乙酰化最初在组蛋白上被发现，并在染色质和 DNA 代谢（如转录、复制和修复）的背景下得到了广泛研究。然而，最近的研究表明，乙酰化比最初想象的更为普遍，它调节各种核以及细胞质和线粒体过程。在这篇综述中，我们介绍了被大型保守 MYST 家族的赖氨酸乙酰转移酶靶向的多种非组蛋白蛋白质，以及这种乙酰化的已知功能后果。MYST 酶的底物包括参与转录、异染色质形成和细胞周期、DNA 修复蛋白、糖异生酶以及 MYST 蛋白复合物本身的亚基的因子。发现 MYST 蛋白的新底物对于理解这些必需乙酰转移酶在核过程、信号转导、应激反应和代谢中的多种功能至关重要。
