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Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled

To be able to quickly and accurately respond to the environment, cells need to tightly control the amount and localization of plasma membrane proteins. The post-translation modification by the protein modifier ubiquitin is the key signal for guiding membrane-associated cargo to the lysosome/vacuole...

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Autor principal: Korbei, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9400068/
https://www.ncbi.nlm.nih.gov/pubmed/35352804
http://dx.doi.org/10.1042/EBC20210042
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author Korbei, Barbara
author_facet Korbei, Barbara
author_sort Korbei, Barbara
collection PubMed
description To be able to quickly and accurately respond to the environment, cells need to tightly control the amount and localization of plasma membrane proteins. The post-translation modification by the protein modifier ubiquitin is the key signal for guiding membrane-associated cargo to the lysosome/vacuole for their degradation. The machinery responsible for such sorting contains several subunits that function as ubiquitin receptors, many of which are themselves subjected to ubiquitination. This review will focus on what is currently known about the modulation of the machinery itself by ubiquitination and how this might affect its function with a special emphasis on current findings from the plant field.
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spelling pubmed-94000682022-08-29 Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled Korbei, Barbara Essays Biochem Plant Biology To be able to quickly and accurately respond to the environment, cells need to tightly control the amount and localization of plasma membrane proteins. The post-translation modification by the protein modifier ubiquitin is the key signal for guiding membrane-associated cargo to the lysosome/vacuole for their degradation. The machinery responsible for such sorting contains several subunits that function as ubiquitin receptors, many of which are themselves subjected to ubiquitination. This review will focus on what is currently known about the modulation of the machinery itself by ubiquitination and how this might affect its function with a special emphasis on current findings from the plant field. Portland Press Ltd. 2022-08 2022-08-05 /pmc/articles/PMC9400068/ /pubmed/35352804 http://dx.doi.org/10.1042/EBC20210042 Text en © 2022 The Author(s). https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Plant Biology
Korbei, Barbara
Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title_full Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title_fullStr Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title_full_unstemmed Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title_short Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
title_sort ubiquitination of the ubiquitin-binding machinery: how early escrt components are controlled
topic Plant Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9400068/
https://www.ncbi.nlm.nih.gov/pubmed/35352804
http://dx.doi.org/10.1042/EBC20210042
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