Proteomic analysis of mTOR inhibition- mediated phosphorylation changes in ribosomal proteins and eukaryotic translation initiation factors

作     者：Xu Jiang Shan Feng Yuling Chen Yun Feng Haiteng Deng 

作者机构：MOE Key Laboratory of Bioinformatics School of Life SciencesTsinghua University Beijing 100084 China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2016年第7卷第7期

页      面：533-537页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 0836[工学-生物工程] 090102[农学-作物遗传育种] 

基　　金：the National Natural Science Foundation of China (Grant No. 31270871 to H.T.D) and MOEC 2012Z02293 (H.T. D)  the National Basic Research Program (973 Program) (No. 2014CBA02005 to H.T.D.) and the Global Science Alliance Program of Thermo-Fisher Scientific 

主　　题：Phosphorylation Site Rapamycin Treatment Eukaryotic Translation Initiation Factor Mediate Phosphorylation Phosphorylation Peptide 

摘      要：Dear Editor, The mammalian target of rapamycin （mTOR）, as a critical energy sensor and cell-growth regulator, controls protein synthesis, autophagy and many important cellular processes through forming functional distinct complexes, mTORC1 and mTORC2, mTORC1 that is sensitive to rapamycin, regulates cell growth and protein synthesis, while mTORC2 that is insensitive to rapamycin, regulates cellular metabolism and the cytoskeletal organization （Gingras et al., 2001; Hay and Sonenberg, 2004）. Translation initiation is the rate-limiting step in protein synthesis, which proceeds through a multi- step process that can be divided into three major steps. First, eukaryotic translation initiation factor 2 （elF2） binds with GTP and methionyl-tRNA to form the ternary complex, which further binds to 40S ribosomal subunit with the help of elF1, elF1A, elF3 and elF5 resulting the preinitiation complex （PIC）. Second, the PIC binds to mRNA which is unwinded by the elF4F complex （including elF4E, elF4G, elF4A, elF4B）.