Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD.
J Cell Biol. 2021 Jan 4;220(1). doi: 10.1083/jcb.202012041.
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.
去除膜蛋白通常需要识别其在脂质双层中的跨膜结构域 (TMD)。在本期中，Arines 等人（2020. J. Cell Biol. https://doi.org/10.1083/jcb.202001116）表明，在酿酒酵母中，液泡相关的 Rsp5 泛素连接酶利用底物衔接子 Ssh4 中的 TMD 识别 Ypq1 中的膜螺旋，这将赖氨酸转运蛋白作为赖氨酸饥饿期间溶酶体降解的靶点。
