Adams, David S.
Endoplasmic reticulum (ER) stress is caused by the accumulation of misfolded proteins in the ER. IRE1, an ER localized transmembrane protein kinase, is a sensor of unfolded proteins and plays an important role in regulating the cellular rescue response to ER stress. We have engineered FV2E-IRE1a, a drug controlled receptor that exploits the IRE1 cell rescue pathway. Addition of the drug AP20187 induces stress-uncoupled activation of FV2E IRE1 and causes IRE1 signaling. Our results indicate that the use of this system has utility in regulating the cytoprotective IRE1-ERAD pathway independently of other ER stress-induced signals, such as proapototic JNK signaling.
Worcester Polytechnic Institute
Major Qualifying Project
All authors have granted to WPI a nonexclusive royalty-free license to distribute copies of the work, subject to other agreements. Copyright is held by the author or authors, with all rights reserved, unless otherwise noted.
Biology and Biotechnology