NDLI: Endoplasmic reticulum stress-mediated induction of SESTRIN 2 potentiates cell survival

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Endoplasmic reticulum stress-mediated induction of SESTRIN 2 potentiates cell survival

Content Provider	Semantic Scholar
Author	Saveljeva, Svetlana Cleary, Patricia A. Mnich, Katarzyna Ayo, Abiodun Pakos-Zebrucka, Karolina Patterson, John B. Logue, Susan E. Samali, Afshin
Copyright Year	2016
Abstract	Upregulation of SESTRIN 2 (SESN2) has been reported in response to diverse cellular stresses. In this study we demonstrate SESTRIN 2 induction following endoplasmic reticulum (ER) stress. ER stress-induced increases in SESTRIN 2 expression were dependent on both PERK and IRE1/XBP1 arms of the unfolded protein response (UPR). SESTRIN 2 induction, post ER stress, was responsible for mTORC1 inactivation and contributed to autophagy induction. Conversely, knockdown of SESTRIN 2 prolonged mTORC1 signaling, repressed autophagy and increased ER stress-induced cell death. Unexpectedly, the increase in ER stress-induced cell death was not linked to autophagy inhibition. Analysis of UPR pathways identified prolonged eIF2α, ATF4 and CHOP signaling in SESTRIN 2 knockdown cells following ER stress. SESTRIN 2 regulation enables UPR derived signals to indirectly control mTORC1 activity shutting down protein translation thus preventing further exacerbation of ER stress.
Starting Page	12254
Ending Page	12266
Page Count	13
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.oncotarget.com/index.php?journal=oncotarget&op=download&page=article&path%5B%5D=7601&path%5B%5D=21993
PubMed reference number	26930721v1
Alternate Webpage(s)	https://doi.org/10.18632/oncotarget.7601
DOI	10.18632/oncotarget.7601
Journal	Oncotarget
Volume Number	7
Language	English
Access Restriction	Open
Subject Keyword	ATF4 gene Alveolar rhabdomyosarcoma Autophagy Cell Death Cell Survival Cessation of life Endoplasmic Reticulum Protein Biosynthesis SESN2 gene cellular response to unfolded protein
Content Type	Text
Resource Type	Article

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