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组蛋白乙酰化(histone acetylation)是调控染色质重塑和真核细胞基因转录的表现遗传修饰(epigenetic modifications)的机制之一。组蛋白乙酰基转移酶(histone acetyltransferase,HAT)和组蛋白去乙酰化酶(histone deacetylase,HDAC)是调节组蛋白N端赖氨酸残基乙酰化或去乙酰化的关键因子。而Ⅱ类HDAC能以磷酸化依赖的方式穿梭于细胞质和细胞核之间,完成组蛋白去乙酰化过程,干扰转录因子并抑制靶基因的转录。因此,研究HDAC磷酸化依赖性核浆穿梭的调节机制具有重要意义。本文简单介绍HDAC5磷酸化依赖性核浆穿梭的调节机制。
Histone acetylation is one of the mechanisms that mediates epigenetic modifications of chromatin remodeling and eukaryotic gene transcription. Histone acetyltransferase (HAT) and histone deacetylase (HDAC) are key factors that regulate the acetylation or deacetylation of N-terminal lysine residues in histones. Class II HDAC can shuttle in the phosphorylation-dependent manner between the cytoplasm and the nucleus to complete the histone deacetylation process, interfere with the transcription factor and inhibit the transcription of the target gene. Therefore, the study of HDAC phosphorylation-dependent regulation of nuclear shuttle system is of great significance. This article briefly describes the regulatory mechanism of HDAC5 phosphorylation-dependent nuclear plasma shuttle.