Yang X-J, Seto E
Molecular Oncology Group, Department of Medicine, McGill University Health Center, Montréal, Québec, Canada.
Oncogene. 2007 Aug 13;26(37):5310-8. doi: 10.1038/sj.onc.1210599.
Acetylation of the epsilon-amino group of a lysine residue was first discovered with histones in 1968, but the responsible enzymes, histone acetyltransferases and deacetylases, were not identified until the mid-1990s. In the past decade, knowledge about this modification has exploded, with targets rapidly expanding from histones to transcription factors and other nuclear proteins, and then to cytoskeleton, metabolic enzymes, and signaling regulators in the cytoplasm. Thus, protein lysine acetylation has emerged as a major post-translational modification to rival phosphorylation. In this issue of Oncogene, 19 articles review various aspects of the enzymes governing lysine acetylation, especially about their intimate links to cancer. To introduce the articles, we highlight here four central themes: (i) multisubunit enzymatic complexes; (ii) non-histone substrates in diverse cellular processes; (iii) interplay of lysine acetylation with other regulatory mechanisms, such as noncoding RNA-mediated gene silencing and activation; and (iv) novel therapeutic strategies and preventive measures to combat cancer and other human diseases.
赖氨酸残基ε-氨基的乙酰化于1968年在组蛋白中首次被发现，但直到20世纪90年代中期，相关的负责酶，即组蛋白乙酰转移酶和去乙酰化酶才被鉴定出来。在过去十年中，关于这种修饰的知识呈爆发式增长，其作用靶点迅速从组蛋白扩展到转录因子和其他核蛋白，进而扩展到细胞骨架、代谢酶以及细胞质中的信号调节因子。因此，蛋白质赖氨酸乙酰化已成为一种主要的翻译后修饰，可与磷酸化相媲美。在本期《癌基因》杂志中，19篇文章综述了调控赖氨酸乙酰化的酶的各个方面，特别是它们与癌症的密切联系。为介绍这些文章，我们在此突出四个核心主题：（i）多亚基酶复合物；（ii）不同细胞过程中的非组蛋白底物；（iii）赖氨酸乙酰化与其他调控机制（如非编码RNA介导的基因沉默和激活）的相互作用；以及（iv）对抗癌症和其他人类疾病的新型治疗策略和预防措施。
