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Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3348923/ https://www.ncbi.nlm.nih.gov/pubmed/22590560 http://dx.doi.org/10.1371/journal.pone.0036542 |
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author | Blount, Jessica R. Burr, Aaron A. Denuc, Amanda Marfany, Gemma Todi, Sokol V. |
author_facet | Blount, Jessica R. Burr, Aaron A. Denuc, Amanda Marfany, Gemma Todi, Sokol V. |
author_sort | Blount, Jessica R. |
collection | PubMed |
description | Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It is not well understood how ubiquitination of ERAD substrates is regulated. Here, we present evidence that the deubiquitinating enzyme Ubiquitin-Specific Protease 25 (USP25) is involved in ERAD. Our data support a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome. |
format | Online Article Text |
id | pubmed-3348923 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33489232012-05-15 Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation Blount, Jessica R. Burr, Aaron A. Denuc, Amanda Marfany, Gemma Todi, Sokol V. PLoS One Research Article Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It is not well understood how ubiquitination of ERAD substrates is regulated. Here, we present evidence that the deubiquitinating enzyme Ubiquitin-Specific Protease 25 (USP25) is involved in ERAD. Our data support a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome. Public Library of Science 2012-05-09 /pmc/articles/PMC3348923/ /pubmed/22590560 http://dx.doi.org/10.1371/journal.pone.0036542 Text en Blount et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Blount, Jessica R. Burr, Aaron A. Denuc, Amanda Marfany, Gemma Todi, Sokol V. Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title | Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title_full | Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title_fullStr | Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title_full_unstemmed | Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title_short | Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation |
title_sort | ubiquitin-specific protease 25 functions in endoplasmic reticulum-associated degradation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3348923/ https://www.ncbi.nlm.nih.gov/pubmed/22590560 http://dx.doi.org/10.1371/journal.pone.0036542 |
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