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Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase

ESCRT-III executes membrane scission during the budding of intralumenal vesicles (ILVs) at endosomes. The scission mechanism is unknown but appears to be linked to the cycle of assembly and disassembly of ESCRT-III complexes at membranes. Regulating this cycle is therefore expected to be important f...

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Autores principales: Johnson, Natalie, West, Matt, Odorizzi, Greg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5328624/
https://www.ncbi.nlm.nih.gov/pubmed/28057764
http://dx.doi.org/10.1091/mbc.E16-11-0761
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author Johnson, Natalie
West, Matt
Odorizzi, Greg
author_facet Johnson, Natalie
West, Matt
Odorizzi, Greg
author_sort Johnson, Natalie
collection PubMed
description ESCRT-III executes membrane scission during the budding of intralumenal vesicles (ILVs) at endosomes. The scission mechanism is unknown but appears to be linked to the cycle of assembly and disassembly of ESCRT-III complexes at membranes. Regulating this cycle is therefore expected to be important for determining the timing of ESCRT-III–mediated membrane scission. We show that in Saccharomyces cerevisiae, ESCRT-III complexes are stabilized and ILV membrane scission is delayed by Doa4, which is the ubiquitin hydrolase that deubiquitinates transmembrane proteins sorted as cargoes into ILVs. These results suggest a mechanism to delay ILV budding while cargoes undergo deubiquitination. We further show that deubiquitination of ILV cargoes is inhibited via Doa4 binding to Vps20, which is the subunit of ESCRT-III that initiates assembly of the complex. Current models suggest that ESCRT-III complexes surround ubiquitinated cargoes to trap them at the site of ILV budding while the cargoes undergo deubiquitination. Thus our results also propose a mechanism to prevent the onset of ILV cargo deubiquitination at the initiation of ESCRT-III complex assembly.
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spelling pubmed-53286242017-05-16 Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase Johnson, Natalie West, Matt Odorizzi, Greg Mol Biol Cell Articles ESCRT-III executes membrane scission during the budding of intralumenal vesicles (ILVs) at endosomes. The scission mechanism is unknown but appears to be linked to the cycle of assembly and disassembly of ESCRT-III complexes at membranes. Regulating this cycle is therefore expected to be important for determining the timing of ESCRT-III–mediated membrane scission. We show that in Saccharomyces cerevisiae, ESCRT-III complexes are stabilized and ILV membrane scission is delayed by Doa4, which is the ubiquitin hydrolase that deubiquitinates transmembrane proteins sorted as cargoes into ILVs. These results suggest a mechanism to delay ILV budding while cargoes undergo deubiquitination. We further show that deubiquitination of ILV cargoes is inhibited via Doa4 binding to Vps20, which is the subunit of ESCRT-III that initiates assembly of the complex. Current models suggest that ESCRT-III complexes surround ubiquitinated cargoes to trap them at the site of ILV budding while the cargoes undergo deubiquitination. Thus our results also propose a mechanism to prevent the onset of ILV cargo deubiquitination at the initiation of ESCRT-III complex assembly. The American Society for Cell Biology 2017-03-01 /pmc/articles/PMC5328624/ /pubmed/28057764 http://dx.doi.org/10.1091/mbc.E16-11-0761 Text en © 2017 Johnson et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Johnson, Natalie
West, Matt
Odorizzi, Greg
Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title_full Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title_fullStr Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title_full_unstemmed Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title_short Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase
title_sort regulation of yeast escrt-iii membrane scission activity by the doa4 ubiquitin hydrolase
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5328624/
https://www.ncbi.nlm.nih.gov/pubmed/28057764
http://dx.doi.org/10.1091/mbc.E16-11-0761
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