Journal
CELL
Volume 164, Issue 1-2, Pages 103-114Publisher
CELL PRESS
DOI: 10.1016/j.cell.2015.11.053
Keywords
-
Categories
Funding
- Adams Fellowship Program of the Israel Academy of Sciences and Humanities
- Adelis Foundation
- Berlin Family Foundation
- NIH [R01GM041223]
- Minerva Foundation
- Israeli Science Foundation
Ask authors/readers for more resources
Translocation into the endoplasmic reticulum (ER) is the first step in the biogenesis of thousands of eukaryotic endomembrane proteins. Although functional ER translocation has been avidly studied, little is known about the quality control mechanisms that resolve faulty translocational states. One such faulty state is translocon clogging, in which the substrate fails to properly translocate and obstructs the translocon pore. To shed light on the machinery required to resolve clogging, we carried out a systematic screen in Saccharomyces cerevisiae that highlighted a role for the ER metalloprotease Ste24. We could demonstrate that Ste24 approaches the translocon upon clogging, and it interacts with and generates cleavage fragments of the clogged protein. Importantly, these functions are conserved in the human homolog, ZMPSTE24, although disease-associated mutant forms of ZMPSTE24 fail to clear the translocon. These results shed light on a new and critical task of Ste24, which safeguards the essential process of translocation.
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