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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Hackett, Anthony J.

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042605-010126

Advisor

• Adams, David S.

Year

• 2005

Sponsor

• Fumihiko Urano
• University of Massachusetts Medical Center.

Date created

• 2005-04-26

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright