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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2022
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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. |
format | Online Article Text |
id | pubmed-9400068 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT korbeibarbara ubiquitinationoftheubiquitinbindingmachineryhowearlyescrtcomponentsarecontrolled |