Open AccessER Stress Activates the TOR Pathway through Atf6
Author(s) -
Dylan Allen,
Jin Ho Seo
Publication year - 2018
Publication title -
journal of molecular signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.721
H-Index - 31
ISSN - 1750-2187
DOI - 10.5334/1750-2187-13-1
Subject(s) - unfolded protein response , endoplasmic reticulum , microbiology and biotechnology , tor signaling , atf6 , crosstalk , biology , signal transduction , proteases , transcription factor , transmembrane protein , genetics , enzyme , biochemistry , receptor , gene , physics , optics
Cellular signaling pathways are often interconnected. They accurately and efficiently regulate essential cell functions such as protein synthesis, cell growth, and survival. The target of rapamycin (TOR) signaling pathway and the endoplasmic reticulum (ER) stress response pathway regulate similar cellular processes. However, the crosstalk between them has not been appreciated until recently and the detailed mechanisms remain unclear. Here, we show that ER stress-inducing drugs activate the TOR signaling pathway in S2R+ Drosophila cells. Activating transcription factor 6 (Atf6), a major stress-responsive ER transmembrane protein, is responsible for ER stress-induced TOR activation. Supporting the finding, we further show that knocking down of both site-1/2 proteases (S1P/S2P), Atf6 processing enzymes, are necessary to connect the two pathways.