Guerra-Calderas Lissania, González-Barrios Rodrigo, Herrera Luis A, Cantú de León David, Soto-Reyes Ernesto
Unidad de Investigación Biomédica en Cáncer, Instituto Nacional de Cancerología-Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City, Mexico.
Unidad de Investigación Biomédica en Cáncer, Instituto Nacional de Cancerología-Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City, Mexico.
Cancer Genet. 2015 May;208(5):215-24. doi: 10.1016/j.cancergen.2014.11.001. Epub 2014 Nov 20.
Histone posttranslational modifications are important components of epigenetic regulation. One extensively studied modification is the methylation of lysine residues. These modifications were thought to be irreversible. However, several proteins with histone lysine demethylase functions have been discovered and characterized. Among these proteins, KDM4A is the first histone lysine demethylase shown to demethylate trimethylated residues. This enzyme plays an important role in gene expression, cellular differentiation, and animal development. Recently, it has also been shown to be involved in cancer. In this review, we focus on describing the structure, mechanisms, and function of KDM4A. We primarily discuss the role of KDM4A in cancer development and the importance of KDM4A as a potential therapeutic target.
组蛋白翻译后修饰是表观遗传调控的重要组成部分。一种被广泛研究的修饰是赖氨酸残基的甲基化。这些修饰曾被认为是不可逆的。然而，已经发现并鉴定了几种具有组蛋白赖氨酸去甲基化酶功能的蛋白质。在这些蛋白质中，KDM4A是首个被证明可使三甲基化残基去甲基化的组蛋白赖氨酸去甲基化酶。这种酶在基因表达、细胞分化和动物发育中发挥重要作用。最近，还发现它与癌症有关。在这篇综述中，我们着重描述KDM4A的结构、机制和功能。我们主要讨论KDM4A在癌症发展中的作用以及KDM4A作为潜在治疗靶点的重要性。
