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Article: Enzymatic blockade of the ubiquitin-proteasome pathway.

TitleEnzymatic blockade of the ubiquitin-proteasome pathway.
Authors
Issue Date2011
Citation
Plos Biology, 2011, v. 8 n. 3, p. e1000605 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.
Persistent Identifierhttp://hdl.handle.net/10722/188684
ISSN
2015 Impact Factor: 8.668
2015 SCImago Journal Rankings: 5.293

 

DC FieldValueLanguage
dc.contributor.authorErnst, Ren_US
dc.contributor.authorClaessen, JHen_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. 8 n. 3, p. e1000605en_US
dc.identifier.issn1545-7885en_US
dc.identifier.urihttp://hdl.handle.net/10722/188684-
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.en_US
dc.languageengen_US
dc.relation.ispartofPLoS biologyen_US
dc.subject.meshBiocatalysisen_US
dc.subject.meshCell Lineen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshGlycoproteins - Metabolismen_US
dc.subject.meshHerpesvirus 4, Human - Enzymologyen_US
dc.subject.meshHumansen_US
dc.subject.meshMolecular Chaperones - Metabolismen_US
dc.subject.meshProteasome Endopeptidase Complex - Metabolismen_US
dc.subject.meshProtein Foldingen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshSignal Transductionen_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshUbiquitin - Metabolismen_US
dc.subject.meshViral Proteins - Metabolismen_US
dc.titleEnzymatic blockade of the ubiquitin-proteasome pathway.en_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.pmid21468303-
dc.identifier.scopuseid_2-s2.0-80053189398en_US
dc.identifier.volume8en_US
dc.identifier.issue3en_US
dc.identifier.spagee1000605en_US
dc.identifier.f100010176956-
dc.identifier.scopusauthoridErnst, R=7201529180en_US
dc.identifier.scopusauthoridClaessen, JH=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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