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Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes
Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light. However, a clear understanding of ubiquitin-dependent protein localization cannot be achieved without knowled...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2006
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063856/ https://www.ncbi.nlm.nih.gov/pubmed/16702236 http://dx.doi.org/10.1083/jcb.200602082 |
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author | Millard, Susan M. Wood, Stephen A. |
author_facet | Millard, Susan M. Wood, Stephen A. |
author_sort | Millard, Susan M. |
collection | PubMed |
description | Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light. However, a clear understanding of ubiquitin-dependent protein localization cannot be achieved without knowledge of the role of deubiquitylating enzymes (DUBs). DUBs, by definition, function downstream in ubiquitin pathways and, as such, have the potential to be the final editors of protein ubiquitylation status, thus determining substrate fate. This paper assimilates the current evidence concerning the substrates and activities of DUBs that regulate protein trafficking. |
format | Text |
id | pubmed-2063856 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20638562007-11-29 Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes Millard, Susan M. Wood, Stephen A. J Cell Biol Reviews Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light. However, a clear understanding of ubiquitin-dependent protein localization cannot be achieved without knowledge of the role of deubiquitylating enzymes (DUBs). DUBs, by definition, function downstream in ubiquitin pathways and, as such, have the potential to be the final editors of protein ubiquitylation status, thus determining substrate fate. This paper assimilates the current evidence concerning the substrates and activities of DUBs that regulate protein trafficking. The Rockefeller University Press 2006-05-22 /pmc/articles/PMC2063856/ /pubmed/16702236 http://dx.doi.org/10.1083/jcb.200602082 Text en Copyright © 2006, The Rockefeller University Press 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 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Reviews Millard, Susan M. Wood, Stephen A. Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title | Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title_full | Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title_fullStr | Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title_full_unstemmed | Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title_short | Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes |
title_sort | riding the dubway: regulation of protein trafficking by deubiquitylating enzymes |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063856/ https://www.ncbi.nlm.nih.gov/pubmed/16702236 http://dx.doi.org/10.1083/jcb.200602082 |
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