mTOR regulates the nucleoplasmic diffusion of Xrn2 under conditions of heat stress

被引：10

作者：

Watanabe, Kazunori ^{[1
,2
]}

Ijiri, Kenichi ^{[2
]}

Ohtsuki, Takashi ^{[1
]}

机构：

[1] Okayama Univ, Grad Sch Nat Sci & Technol, Dept Biotechnol, Okayama, Japan

[2] Univ Tokyo, Radioisotope Ctr, Tokyo, Japan

来源：

FEBS LETTERS | 2014年 / 588卷 / 18期

关键词：

Mammalian target of rapamycin; tRNA degradation; Xrn2; Heat stress; REPLICATION PROTEIN-A; TRANSFER-RNA; OXIDATIVE STRESS; TRANSLATION INITIATION; GRANULE FORMATION; DNA-REPLICATION; SHOCK RESPONSE; ANGIOGENIN; RAPAMYCIN; COMPLEX;

D O I：

10.1016/j.febslet.2014.08.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Stress induces various responses, including translational suppression and tRNA degradation in mammals. Previously, we showed that heat stress induces degradation of initiator tRNA(Met) (iMet) through 5'-3' exoribonuclease Xrn1 and Xrn2, respectively. In addition, we found that rapamycin inhibits the degradation of iMet under heat stress conditions. Here, we report that the mammalian target of rapamycin (mTOR) regulates the diffusion of Xrn2 from the nucleolus to the nucleoplasm, facilitating the degradation of iMet under conditions of heat stress. Our results suggest a mechanism of translational suppression through mTOR-regulated iMet degradation in mammalian cells. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3454 / 3460

页数：7

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