Leucine induced dephosphorylation of Sestrin2 promotes mTORC1 activation
详细信息 查看全文
- 作者：Scot R. Kimball ; 1 ; skimball@psu.edu" class="auth_mail" title="E-mail the corresponding author ; Bradley S. Gordon1 ; 2 ; Jenna E. Moyer ; Michael D. Dennis ; Leonard S. Jefferson
- 关键词：4E-BP1 ; eukaryotic initiation factor 4E binding protein 1 ; AMPK ; AMP-activated protein kinase ; Atg13 ; autophagy-related 13 ; FIP200 ; 200 ; kilodalton focal adhesion kinase family kinase-interacting protein ; GAP ; GTPase activator protein ; GATOR ; GAP activity toward Rags ; LARS ; leucyl-tRNA synthetase ; MEF ; mouse embryo fibroblasts ; mTOR ; mechanistic target of rapamycin ; mTORC1 ; mTOR complex 1 ; p70S6K1 ; 70 ; kDa ribosomal protein S6 kinase 1 ; PP2A ; protein phosphatase 2A ; Rag ; Ras-related GTP
- 刊名：Cellular Signalling
- 出版年：2016
- 出版时间：August 2016
- 年：2016
- 卷：28
- 期：8
- 页码：896-906
- 全文大小：1455 K
文摘
- •
Deprivation of leucine led to a reduction in the electrophoretic mobility of Sestrin2.
- •
Reduced electrophoretic mobility was due to increased phosphorylation.
- •
Sestrin2 phosphorylation was independent of mTORC1, but dependent upon ULK1.
- •
Sites of Sestrin2 phosphorylation were identified as Thr232, Ser249, and Ser279.
- •
A phospho-mimetic Sestrin2 variant repressed mTORC1 in a leucine-independent manner.