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Comment
. 2021 Jan 4;220(1):e202012041.
doi: 10.1083/jcb.202012041.

Chaperoning transmembrane helices in the lipid bilayer

Qi Zhang  1 , Yihong Ye  1
Affiliations
Comment

Chaperoning transmembrane helices in the lipid bilayer

Qi Zhang et al. J Cell Biol. .

Abstract

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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Figures

Figure 1.
Figure 1.
Regulated recognition of Ypq1 by Ssh4. When lysine in the cytosol is abundant, Ypq1 undergoes a rapid conformational cycle to transport lysine from the cytosol into the vacuole lumen. Under lysine-depleted conditions, the transporter is trapped in a conformation recognizable by Ssh4, which recruits Rsp5 to catalyze Ypq1 ubiquitination and internalization into the MVB. Ub, ubiquitin.
See this image and copyright information in PMC

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