Ubiquitin-specific protease USP25 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...

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Detalles Bibliográficos
Autores: Blount, J. R., Burr, A. A., Denuc Isern, Amanda, Marfany i Nadal, Gemma, Todi, S. V.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2012
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/43320
Acceso en línea:https://hdl.handle.net/2445/43320
Access Level:acceso abierto
Palabra clave:Proteïnes
Enzims
Reticle endoplasmàtic
Proteins
Enzymes
Endoplasmic reticulum
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spelling Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradationBlount, J. R.Burr, A. A.Denuc Isern, AmandaMarfany i Nadal, GemmaTodi, S. V.ProteïnesEnzimsReticle endoplasmàticProteinsEnzymesEndoplasmic reticulumEndoplasmic 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 (PLoS)2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/43320Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0036542PLoS One, 2012, vol. 7, num. 5, p. e36542http://dx.doi.org/10.1371/journal.pone.0036542cc-by (c) Blount, J.R. et al., 2012http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/433202026-05-27T06:46:51Z
dc.title.none.fl_str_mv Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
title Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
spellingShingle Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
Blount, J. R.
Proteïnes
Enzims
Reticle endoplasmàtic
Proteins
Enzymes
Endoplasmic reticulum
title_short Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
title_full Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
title_fullStr Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
title_full_unstemmed Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
title_sort Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
dc.creator.none.fl_str_mv Blount, J. R.
Burr, A. A.
Denuc Isern, Amanda
Marfany i Nadal, Gemma
Todi, S. V.
author Blount, J. R.
author_facet Blount, J. R.
Burr, A. A.
Denuc Isern, Amanda
Marfany i Nadal, Gemma
Todi, S. V.
author_role author
author2 Burr, A. A.
Denuc Isern, Amanda
Marfany i Nadal, Gemma
Todi, S. V.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Proteïnes
Enzims
Reticle endoplasmàtic
Proteins
Enzymes
Endoplasmic reticulum
topic Proteïnes
Enzims
Reticle endoplasmàtic
Proteins
Enzymes
Endoplasmic reticulum
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.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/43320
url https://hdl.handle.net/2445/43320
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0036542
PLoS One, 2012, vol. 7, num. 5, p. e36542
http://dx.doi.org/10.1371/journal.pone.0036542
dc.rights.none.fl_str_mv cc-by (c) Blount, J.R. et al., 2012
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Blount, J.R. et al., 2012
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library of Science (PLoS)
publisher.none.fl_str_mv Public Library of Science (PLoS)
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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