[蛋白激酶A底物40 kDa的研究进展]
[Research progress in PRAS40].
作者信息
Chen Gang, Zhu Gangcai, Zhang Xin
机构信息
Department of Otorhinolaryngology Head and Neck Surgery, Second Xiangya Hospital, Central South University, Changsha 410011, China.
出版信息
Zhong Nan Da Xue Xue Bao Yi Xue Ban. 2018 Jun 28;43(6):685-690. doi: 10.11817/j.issn.1672-7347.2018.06.017.
Prolin-rich Akt substrate of 40 kD (PRAS40) is firstly identified as a partner of 14-3-3 protein and a substrate of Akt kinase by Roth et al in 2003. Accumulated evidence shows that PRAS40 is mainly activated by phosphorylate modification at different sites. PRAS40 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.
富含脯氨酸的40kD Akt底物（PRAS40）于2003年被罗斯等人首次鉴定为14-3-3蛋白的伴侣和Akt激酶的底物。越来越多的证据表明，PRAS40主要通过不同位点的磷酸化修饰而被激活。PRAS40可能参与多种信号通路，如哺乳动物雷帕霉素靶蛋白复合物1（mTORC1）、蛋白激酶B（Akt）、核因子κB（NF-κB）和核糖体蛋白L11（RPL11）等，这些信号通路可调节细胞增殖、衰老、自噬、凋亡和外泌体分泌。
Zotero 插件