酸化MAP激酶ERK2促进其同位体化和核转位
A V Khokhlatchev1, B Canagarajah, J Wilsbacher
1Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas 75235-9041, USA.
Cell
|May 30, 1998
概括
MAP激酶ERK2的核积累取决于其酸化状态,而不是其活性. 核转移所必需的二元化,由酸化促进,并通过晶体结构分析揭示出来.
科学领域:
- 蜂信号传输是如何进行的
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 线素激活蛋白 (MAP) 激酶ERK2在真核生物信号传导途径中至关重要.
- 激活的ERK2转移到核中以酸化核标,调节基因表达和细胞反应.
研究的目的:
- 调查控制ERK2.2核积累的因素.
- 确定酸化,活性和二聚化在ERK2核转移中的作用.
主要方法:
- 在细胞中微注射ERK2.
- 改变ERK2的突变,以破坏二分化.
- 对ERK2局部化和酸化状态的分析.
- 化ERK2.2的晶体结构的确定.
主要成果:
- 微注射ERK2的核积累取决于其酸化状态,而不是其激酶活性或上游信号组件.
- 酸化ERK2与酸化和非酸化ERK2形成二元体.
- 破坏ERK2二分化会显著减少其核积累,这表明二分化对于核重新定位至关重要.
- 化ERK2的晶体结构阐明了二分化过程的分子基础.
结论:
- 酸化依赖的二分化是ERK2核转位的关键机制.
- 模化对于ERK2.2的正常依赖连接体的重新定位至关重要.
- 分化可能是MAP激酶家族的一般作用机制.
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