National Brain Research Centre, Manesar, Haryana-122050, India.
Neuroscience. 2010 May 5;167(2):354-60. doi: 10.1016/j.neuroscience.2010.02.023. Epub 2010 Feb 16.
Phosphorylation is critically involved in synaptic plasticity and memory. Recent studies have shown that another posttranslational modification, acetylation, particularly of histone H3, also plays important roles in long-term potentiation and memory. However, activity-dependent modification of different histones of the nucleosome is not clearly understood. Here we show that depolarization enhances acetylation of histone H2B in the CA1 region of the hippocampus. Depolarization-induced H2B acetylation is dependent on calcium/calmodulin-dependent kinase and extracellular signal-regulated kinase activity. In addition, inhibition of DNA methyltransferase activity also abolishes depolarization-induced increase in H2B acetylation. These results show that acetylation of histone H2B is regulated in an activity-dependent manner by the molecular events important for synaptic plasticity and memory.
磷酸化在突触可塑性和记忆中起着至关重要的作用。最近的研究表明，另一种翻译后修饰，乙酰化，特别是组蛋白 H3 的乙酰化，也在长时程增强和记忆中发挥重要作用。然而，核小体不同组蛋白的活性依赖性修饰还不是很清楚。在这里，我们显示去极化增强了海马 CA1 区组蛋白 H2B 的乙酰化。去极化诱导的 H2B 乙酰化依赖于钙/钙调蛋白依赖性激酶和细胞外信号调节激酶活性。此外，抑制 DNA 甲基转移酶活性也会消除去极化诱导的 H2B 乙酰化增加。这些结果表明，组蛋白 H2B 的乙酰化是通过对突触可塑性和记忆很重要的分子事件来进行活性依赖性调节的。
