Journal
JOURNAL OF CELL BIOLOGY
Volume 220, Issue 1, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202012041
Keywords
-
Categories
Funding
- National Institute of Diabetes, Digestive, and Kidney Diseases of National Institutes of Health
Ask authors/readers for more resources
In yeast, the vacuole-associated Rsp5 ubiquitin ligase utilizes a substrate adaptor Ssh4 to recognize membrane helices in Ypq1, targeting the lysine transporter for lysosomal degradation during lysine starvation.
Elimination of membrane proteins often requires recognition of their transmembrane domains (TMDs) in the lipid bilayer. In this issue, Arines et al. (2020. J. Cell Biol. https://doi.org/10.1083/jcb.202001116) show that in Saccharomyces cerevisiae, the vacuole-associated Rsp5 ubiquitin ligase uses a TMD in substrate adaptor Ssh4 to recognize membrane helices in Ypq1, which targets this lysine transporter for lysosomal degradation during lysine starvation.
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