PRAS40蛋白的研究进展  

Research progress in PRAS40

作　　者：陈刚 朱刚才[1] 张欣[1] CHEN Gang;ZHU Gangcai;ZHANG Xin(Department of Otorhinolaryngology Head and Neck Surgery, Second Xiangya Hospital, Central South University, Changsha 410011, China)

机构地区：[1]中南大学湘雅二医院耳鼻叫喉头颈外科,长沙410011

出　　处：《中南大学学报（医学版）》2018年第6期685-690,共6页Journal of Central South University ：Medical Science

基　　金：国家自然科学基金(81772903,81472696,81602389);湖南省自然科学基金(2017JJ3456).

摘　　要：40 kD大小的富含脯氨酸蛋白激酶B(protein kinase B,Akt)底物蛋白(prolin-rich Akt substrate of 40 kD,PRAS40)是2003年Roth等从胞质锚定蛋白14-3-3的伴侣蛋白及Akt激酶的底物中首先鉴定的。PRAS40的活化主要方式为磷酸化修饰,并具有多个磷酸化位点。PRAS40参与调控哺乳动物雷帕霉素靶蛋白复合物1(mammalian target of rapamycin complex 1,mTORC1),Akt,NF-κB和核糖体蛋白L11(ribosomal protein L11,RPL11)等多条信号通路,影响细胞的增殖、衰老、自噬、凋亡、外泌体分泌等。Prolin-rich Akt substrate of 40 kD （PRA S40） is fi rstly identifi ed as a partner of 14-3-3 protein and a substrate of Akt kinase by Roth et al in 2003. Accumulated evidence shows that PRA S40 is mainly activated by phosphorylate modifi cation at diff erent sites. PRA S40 may be involved in various of signaling pathways, such as mammalian target of rapamycin complex 1 （mTORC1）, protein kinase B （Akt）, NF-κB and ribosomal protein L11 （RPL11） etc, which can regulate cell proliferation,senescence, autophagy, apoptosis and exosome secretion.

关 键 词：40 kD大小的富含脯氨酸蛋白激酶B底物蛋白 哺乳动物雷帕霉素靶蛋白复合物1 蛋白激酶B 磷酸化 NF-κB P53 肿瘤 代谢疾病 

分 类 号：R341[医药卫生—基础医学]