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Reading: ER stress activates the TOR pathway through Atf6

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Research Articles

ER stress activates the TOR pathway through Atf6

Authors:

Dylan Allen ,

Rogers State University, US
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Jin Seo

Rogers State University, US
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Abstract

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.
How to Cite: Allen D, Seo J. ER stress activates the TOR pathway through Atf6. Journal of Molecular Signaling. 2017;12.
Published on 04 Aug 2017.
Peer Reviewed

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