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...
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| Veröffentlicht in: | PloS one 2012-05, Vol.7 (5), p.e36542-e36542 |
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| creator | Blount, Jessica R Burr, Aaron A Denuc, Amanda Marfany, Gemma Todi, Sokol V |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0036542 |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0036542</identifier><identifier>PMID: 22590560</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alzheimer's disease ; Animals ; Biology ; Cell division ; Cercopithecus aethiops ; COS Cells ; Degradation ; Endoplasmic reticulum ; Endoplasmic Reticulum - enzymology ; Endoplasmic Reticulum - genetics ; Endoplasmic Reticulum-Associated Degradation - physiology ; Enzymes ; Genomes ; HEK293 Cells ; Humans ; Ligases ; Medicine ; Microscopy ; Mutation ; Neurology ; Neurotoxicity ; Pathogenesis ; Pharmacology ; Post-translational modifications ; Protease ; Proteases ; Proteasome Endopeptidase Complex - genetics ; Proteasome Endopeptidase Complex - metabolism ; Proteasomes ; Proteins ; Proteolysis ; Quality control ; Quality management ; Substrates ; Ubiquitin ; Ubiquitin Thiolesterase - genetics ; Ubiquitin Thiolesterase - metabolism ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitin-specific proteinase ; Ubiquitinated Proteins - genetics ; Ubiquitinated Proteins - metabolism ; Ubiquitination ; Ubiquitination - physiology</subject><ispartof>PloS one, 2012-05, Vol.7 (5), p.e36542-e36542</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Blount et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blount, Jessica R</au><au>Burr, Aaron A</au><au>Denuc, Amanda</au><au>Marfany, Gemma</au><au>Todi, Sokol V</au><au>Menéndez-Arias, Luis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-05-09</date><risdate>2012</risdate><volume>7</volume><issue>5</issue><spage>e36542</spage><epage>e36542</epage><pages>e36542-e36542</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22590560</pmid><doi>10.1371/journal.pone.0036542</doi><tpages>e36542</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alzheimer's disease Animals Biology Cell division Cercopithecus aethiops COS Cells Degradation Endoplasmic reticulum Endoplasmic Reticulum - enzymology Endoplasmic Reticulum - genetics Endoplasmic Reticulum-Associated Degradation - physiology Enzymes Genomes HEK293 Cells Humans Ligases Medicine Microscopy Mutation Neurology Neurotoxicity Pathogenesis Pharmacology Post-translational modifications Protease Proteases Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism Proteasomes Proteins Proteolysis Quality control Quality management Substrates Ubiquitin Ubiquitin Thiolesterase - genetics Ubiquitin Thiolesterase - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitin-specific proteinase Ubiquitinated Proteins - genetics Ubiquitinated Proteins - metabolism Ubiquitination Ubiquitination - physiology |
| title | Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation |
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