Journal
SCIENCE
Volume 346, Issue 6210, Pages 751-755Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1255638
Keywords
-
Categories
Funding
- CRG
- International Early Career Award from the HHMI
- EMBO Young Investigator Program
- Spanish MCCIN
- ERC
Ask authors/readers for more resources
Misfolded proteins in the endoplasmic reticulum (ER) are eliminated by a quality control system called ER-associated protein degradation (ERAD). However, it is unknown how misfolded proteins in the inner nuclear membrane (INM), a specialized ER subdomain, are degraded. We used a quantitative proteomics approach to reveal an ERAD branch required for INM protein quality control in yeast. This branch involved the integral membrane proteins Asi1, Asi2, and Asi3, which assembled into an Asi complex. Besides INM misfolded proteins, the Asi complex promoted the degradation of functional regulators of sterol biosynthesis. Asi-mediated ERAD was required for ER homeostasis, which suggests that spatial segregation of protein quality control systems contributes to ER function.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available