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Article: Enzymatic blockade of the ubiquitin-proteasome pathway

TitleEnzymatic blockade of the ubiquitin-proteasome pathway
Authors
Issue Date2011
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosbiology.org/plosonline/?request=index-html
Citation
Plos Biology, 2011, v. 9 n. 3 How to Cite?
AbstractUbiquitin-dependent processes control much of cellular physiology. We show that expression of a highly active, Epstein-Barr virus-derived deubiquitylating enzyme (EBV-DUB) blocks proteasomal degradation of cytosolic and ER-derived proteins by preemptive removal of ubiquitin from proteasome substrates, a treatment less toxic than the use of proteasome inhibitors. Recognition of misfolded proteins in the ER lumen, their dislocation to the cytosol, and degradation are usually tightly coupled but can be uncoupled by the EBV-DUB: a misfolded glycoprotein that originates in the ER accumulates in association with cytosolic chaperones as a deglycosylated intermediate. Our data underscore the necessity of a DUB activity for completion of the dislocation reaction and provide a new means of inhibition of proteasomal proteolysis with reduced cytotoxicity. © 2011 Ernst et al.
Persistent Identifierhttp://hdl.handle.net/10722/188683
ISSN
2010 Impact Factor: 12.472
2015 SCImago Journal Rankings: 5.293
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorErnst, Ren_US
dc.contributor.authorClaessen, JHLen_US
dc.contributor.authorMueller, Ben_US
dc.contributor.authorSanyal, Sen_US
dc.contributor.authorSpooner, Een_US
dc.contributor.authorVan Der Veen, AGen_US
dc.contributor.authorKirak, Oen_US
dc.contributor.authorSchlieker, CDen_US
dc.contributor.authorWeihofen, WAen_US
dc.contributor.authorPloegh, HLen_US
dc.date.accessioned2013-09-03T04:12:45Z-
dc.date.available2013-09-03T04:12:45Z-
dc.date.issued2011en_US
dc.identifier.citationPlos Biology, 2011, v. 9 n. 3en_US
dc.identifier.issn1544-9173en_US
dc.identifier.urihttp://hdl.handle.net/10722/188683-
dc.description.abstractUbiquitin-dependent processes control much of cellular physiology. We show that expression of a highly active, Epstein-Barr virus-derived deubiquitylating enzyme (EBV-DUB) blocks proteasomal degradation of cytosolic and ER-derived proteins by preemptive removal of ubiquitin from proteasome substrates, a treatment less toxic than the use of proteasome inhibitors. Recognition of misfolded proteins in the ER lumen, their dislocation to the cytosol, and degradation are usually tightly coupled but can be uncoupled by the EBV-DUB: a misfolded glycoprotein that originates in the ER accumulates in association with cytosolic chaperones as a deglycosylated intermediate. Our data underscore the necessity of a DUB activity for completion of the dislocation reaction and provide a new means of inhibition of proteasomal proteolysis with reduced cytotoxicity. © 2011 Ernst et al.en_US
dc.languageengen_US
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosbiology.org/plosonline/?request=index-htmlen_US
dc.relation.ispartofPLoS Biologyen_US
dc.titleEnzymatic blockade of the ubiquitin-proteasome pathwayen_US
dc.typeArticleen_US
dc.identifier.emailSanyal, S: sumana@wi.mit.eduen_US
dc.identifier.authoritySanyal, S=rp01794en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1371/journal.pbio.1000605en_US
dc.identifier.scopuseid_2-s2.0-79953687692en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79953687692&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume9en_US
dc.identifier.issue3en_US
dc.identifier.isiWOS:000288942200009-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridErnst, R=7201529180en_US
dc.identifier.scopusauthoridClaessen, JHL=24734020000en_US
dc.identifier.scopusauthoridMueller, B=15045301300en_US
dc.identifier.scopusauthoridSanyal, S=16069600000en_US
dc.identifier.scopusauthoridSpooner, E=7006184562en_US
dc.identifier.scopusauthoridvan der Veen, AG=14013802800en_US
dc.identifier.scopusauthoridKirak, O=20734685500en_US
dc.identifier.scopusauthoridSchlieker, CD=6602257387en_US
dc.identifier.scopusauthoridWeihofen, WA=35787482900en_US
dc.identifier.scopusauthoridPloegh, HL=35433834100en_US

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