CDK依赖的Hsp70酸化控制了G1环林丰度和细胞循环进展
Andrew W Truman1, Kolbrun Kristjansdottir, Donald Wolfgeher
1Ludwig Center for Metastasis Research, The University of Chicago, Chicago, IL 60637, USA.
Cell
|December 11, 2012
概括
热冲击蛋白70 (Hsp70) 通过循环素依赖激酶 (CDK) 的酸化控制了G1循环素的稳定性和细胞循环的进展. 这种机制在人类中保留,通过调节循环素的丰富性和活性来调节生长.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- Hsp70伴侣蛋白是调节细胞功能的必要蛋白质.
- 它们的活性是由表达,异形和协伴蛋白调节的.
研究的目的:
- 为了研究Hsp70功能的新型调节机制.
- 探索Hsp70酸化在细胞周期控制中的作用.
主要方法:
- 在芽酵母中酸化位点分析Ssa1.1.
- 研究Ssa1,Ydj1和Cln3.3之间的相互作用.
- 研究CDK Pho85和Cdk1对Ssa1酸化和Cln3稳定性的影响.
- 检查人类Hsc70和Cyclin D1.1.中的保存酸化.
主要成果:
- 通过CDKs对Ssa1在T36的酸化改变了cochaperone和客户端的相互作用.
- T36的酸化取代了Ydj1,使Ssa1能够结合并降解G1环林Cln3.
- 压力和线性CDKs (Pho85,Cdk1) 通过Ssa1酸化调节Cln3的稳定性.
- 人类Hsc70 T38的CDK依赖酸化会影响循环D1的稳定性.
结论:
- Hsp70在细胞生长控制中充当信号传感器.
- 通过CDK介导的Hsp70酸化调节了G1环林的丰度和活性.
- 这种酸化机制从酵母保存到人类.
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