Chaperoning transmembrane helices in the lipid bilayer

被引：2

作者：

Zhang, Qi ^{[1
]}

Ye, Yihong ^{[1
]}

机构：

[1] NIDDK, Lab Mol Biol, NIH, Bethesda, MD 20892 USA

来源：

JOURNAL OF CELL BIOLOGY | 2021年 / 220卷 / 01期

基金：

美国国家卫生研究院;

关键词：

UBIQUITIN; PROTEINS; DOMAIN;

D O I：

10.1083/jcb.202012041

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页数：2

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