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ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation
The lysosome (or vacuole in fungi and plants) is an essential organelle for nutrient sensing and cellular homeostasis. In response to environmental stresses such as starvation, the yeast vacuole can adjust its membrane composition by selectively internalizing membrane proteins into the lumen for deg...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8167898/ https://www.ncbi.nlm.nih.gov/pubmed/34047770 http://dx.doi.org/10.1083/jcb.202012104 |
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author | Yang, Xi Reist, Lucas Chomchai, Dominic A. Chen, Liang Arines, Felichi Mae Li, Ming |
author_facet | Yang, Xi Reist, Lucas Chomchai, Dominic A. Chen, Liang Arines, Felichi Mae Li, Ming |
author_sort | Yang, Xi |
collection | PubMed |
description | The lysosome (or vacuole in fungi and plants) is an essential organelle for nutrient sensing and cellular homeostasis. In response to environmental stresses such as starvation, the yeast vacuole can adjust its membrane composition by selectively internalizing membrane proteins into the lumen for degradation. Regarding the selective internalization mechanism, two competing models have been proposed. One model suggests that the ESCRT machinery is responsible for the sorting. In contrast, the ESCRT-independent intralumenal fragment (ILF) pathway proposes that the fragment generated by homotypic vacuole fusion is responsible for the sorting. Here, we applied a microfluidics-based imaging method to capture the complete degradation process in vivo. Combining live-cell imaging with a synchronized ubiquitination system, we demonstrated that ILF cargoes are not degraded through intralumenal fragments. Instead, ESCRTs function on the vacuole membrane to sort them into the lumen for degradation. We further discussed challenges in reconstituting vacuole membrane protein degradation. |
format | Online Article Text |
id | pubmed-8167898 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-81678982022-02-02 ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation Yang, Xi Reist, Lucas Chomchai, Dominic A. Chen, Liang Arines, Felichi Mae Li, Ming J Cell Biol Report The lysosome (or vacuole in fungi and plants) is an essential organelle for nutrient sensing and cellular homeostasis. In response to environmental stresses such as starvation, the yeast vacuole can adjust its membrane composition by selectively internalizing membrane proteins into the lumen for degradation. Regarding the selective internalization mechanism, two competing models have been proposed. One model suggests that the ESCRT machinery is responsible for the sorting. In contrast, the ESCRT-independent intralumenal fragment (ILF) pathway proposes that the fragment generated by homotypic vacuole fusion is responsible for the sorting. Here, we applied a microfluidics-based imaging method to capture the complete degradation process in vivo. Combining live-cell imaging with a synchronized ubiquitination system, we demonstrated that ILF cargoes are not degraded through intralumenal fragments. Instead, ESCRTs function on the vacuole membrane to sort them into the lumen for degradation. We further discussed challenges in reconstituting vacuole membrane protein degradation. Rockefeller University Press 2021-05-28 /pmc/articles/PMC8167898/ /pubmed/34047770 http://dx.doi.org/10.1083/jcb.202012104 Text en © 2021 Yang et al. 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 | Report Yang, Xi Reist, Lucas Chomchai, Dominic A. Chen, Liang Arines, Felichi Mae Li, Ming ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title | ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title_full | ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title_fullStr | ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title_full_unstemmed | ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title_short | ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
title_sort | escrt, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8167898/ https://www.ncbi.nlm.nih.gov/pubmed/34047770 http://dx.doi.org/10.1083/jcb.202012104 |
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