Chaperoning transmembrane helices in the lipid bilayer

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...

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Detalles Bibliográficos
Autores principales: Zhang, Qi, Ye, Yihong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2020
Materias:
Spotlight
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7759301/
https://www.ncbi.nlm.nih.gov/pubmed/33351098
http://dx.doi.org/10.1083/jcb.202012041
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author Zhang, Qi
Ye, Yihong
author_facet Zhang, Qi
Ye, Yihong
author_sort Zhang, Qi
collection PubMed
description 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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spelling pubmed-77593012021-07-04 Chaperoning transmembrane helices in the lipid bilayer Zhang, Qi Ye, Yihong J Cell Biol Spotlight 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. Rockefeller University Press 2020-12-22 /pmc/articles/PMC7759301/ /pubmed/33351098 http://dx.doi.org/10.1083/jcb.202012041 Text en This is a work of the U.S. Government and is not subject to copyright protection in the United States. Foreign copyrights may apply. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Spotlight
Zhang, Qi
Ye, Yihong
Chaperoning transmembrane helices in the lipid bilayer
title Chaperoning transmembrane helices in the lipid bilayer
title_full Chaperoning transmembrane helices in the lipid bilayer
title_fullStr Chaperoning transmembrane helices in the lipid bilayer
title_full_unstemmed Chaperoning transmembrane helices in the lipid bilayer
title_short Chaperoning transmembrane helices in the lipid bilayer
title_sort chaperoning transmembrane helices in the lipid bilayer
topic Spotlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7759301/
https://www.ncbi.nlm.nih.gov/pubmed/33351098
http://dx.doi.org/10.1083/jcb.202012041
work_keys_str_mv AT zhangqi chaperoningtransmembranehelicesinthelipidbilayer
AT yeyihong chaperoningtransmembranehelicesinthelipidbilayer

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