PIM2 regulates stemness through phosphorylation of 4E-BP1

作     者：Hongyan Sun Jiani Cao Lin Zhao Shaohua Zhu Shenghui Chen Yaqiong Li Bin Zhao Tongbiao Zhao 

作者机构：astate Key Laboratory of Stem Cell and Reproductive Biology Institute of Zoology Chinese Academy of Sciences Beijing 100101 China Graduate University of Chinese Academy of Sciences Beijing 100049 China Chinese Medicine Hospital in Linyi City Linyi 276600 China Life Sciences Institute Zhejiang University Hangzhou 310058 China 

出 版 物：《Science Bulletin》 (科学通报（英文版）)

年 卷 期：2017年第62卷第10期

页      面：679-685页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 071009[理学-细胞生物学] 09[农学] 0901[农学-作物学] 090102[农学-作物遗传育种] 

基　　金：supported by the National Basic Research Program of China (2013CB966901) the Strategic Priority Research Program of the Chinese Academy of Sciences (XDA01040108) The National Thousand of Talents Program to T.Z., and the National Natural Science Foundation of China (31570995, 31621004) to T.Z. and (31400831) to J.C 

主　　题：4E BPI ESC Phosphorylation Pim2 Sternness 

摘      要：Embryonic stem cells （ESCs） can undergo unlimited self-renewal and maintain pluripotency to differen- tiate into any cell type of the three germ layers. Extensive studies have shown ESC identity is regulated by transcription factors, epigenetic regulators and multiple signal transduction pathways. However, the kinase regulation of pluripotency is not well understood. Here we show that the serine/threonine kinase PlM2, which is highly expressed in ESCs but not in somatic cells, functions as a crucial stemness regulator in ESCs. Knockout of Pim2 inhibits the self-renewal and differentiation capability of ESCs. Mechanistic studies identified that PIM2 can directly phosphorylate 4E-BP1, leading to release of elF4E which facili- tates the translation of pluripotent genes in ESCs. Our study highlights a novel kinase cascade pathway for ESC identity maintenance.