定量生物学中心学术报告

题目： The Activity and Stability of p21 is Regulated by Non-Receptor Tyrosine Kinases

报告人： 黄永棋 助理研究员

山东大学化学与化工学院物理化学专业

时间：2016-2-24（周三），13:00-14:00

地点：英国威廉希尔公司老化学楼东配楼102会议室

主持人：刘志荣 教授

摘 要:

The Cip/Kip family of cyclin-dependent kinase (Cdk) inhibitors includes p21Cip1, p27Kip1 and p57Kip2. Their kinase inhibitory activities are mediated by a homologous N-terminal kinase-inhibitory domain (KID). The Cdk inhibitory activity and stability of p27 have been shown to be regulated by a two-step phosphorylation mechanism involving a tyrosine residue within the KID and a threonine residue within the flexible C-terminus. We show that these residues are conserved in p21 and p57, suggesting that a similar phosphorylation cascade regulates these Cdk inhibitors. However, the presence of a cyclin binding motif within its C-terminus alters the regulatory interplay between p21 and Cdk2/cyclin A, and its responses to tyrosine phosphorylation and altered p21:Cdk2/cyclin A stoichiometry. Although the Cip/Kip proteins can be phosphorylated in vitro by representatives of many non-receptor tyrosine kinase (NRTK) sub-families, the stability of p21 is not related to tyrosine phosphorylation in cell based experiments, suggesting that the stability and activity of Cip/Kip proteins are regulated via different mechanisms.

报告人简介：黄永棋，男，博士，山东大学化学与化工学院物理化学专业助理研究员。2012年毕业于英国威廉希尔公司化学与分子工程学院物理化学专业，获博士学位。2012-2015年在美国St Jude Children’s Research Hospital结构生物学专业从事博士后研究。2016年1月至今任山东大学化学与化工学院物理化学专业助理研究员。主要研究兴趣是应用分子模拟以及生物实验技术来探索天然无序蛋白质的序列—结构—功能关系。近年来在国际重要学术刊物J mol Biol等以第一作者身份发表论文10余篇。

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