期刊
JOURNAL OF CELL BIOLOGY
卷 220, 期 1, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202012041
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- National Institute of Diabetes, Digestive, and Kidney Diseases of National Institutes of Health
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.
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