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dc.contributor.authorLipinszki, Zoltánen
dc.contributor.authorKovács, Leventeen
dc.contributor.authorDeák, Péteren
dc.contributor.authorUdvardy, Andoren
dc.date.accessioned2019-07-30T23:30:24Z
dc.date.available2019-07-30T23:30:24Z
dc.date.issued2012-03-27en
dc.identifier.issn0006-2960
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/295095
dc.description.abstractAnalysis of the in vivo ubiquitylation of the p54/Rpn10 polyubiquitin receptor subunit of the Drosophila 26S proteasome revealed that the site of ubiquitylation is the C-terminal cluster of lysines, which is conserved in higher eukaryotes. Extraproteasomal p54 was extensively multiubiquitylated, but only very modest modification was detected in the proteasome-assembled subunit. Ubiquitylation of p54 seriously jeopardizes one of its most important functions, i.e., the interaction of its ubiquitin-interacting motifs with the ubiquitin-like domain of Dsk2 and Rad23 extraproteasomal polyubiquitin receptors. This modification of p54 supports the previous notion that p54 is a shuttling subunit of the 26S proteasome with a specific extraproteasomal function. This assumption is supported by the observation that, while transgenic p54 can fully rescue the lethal phenotype of the Δp54 null mutation, its derivative from which the cluster of conserved lysines is deleted shifts the lethality from the early pupa to pharate adult stage but cannot rescue the Δp54 mutation, suggesting that ubiquitylated extraproteasomal p54 has an essential role in the pupa-adult transition.
dc.description.sponsorshipThis work was supported by the Institute of Biochemistry (Biological Research Centre of the Hungarian Academy of Sciences).
dc.languageengen
dc.publisherACS
dc.rightsAll rights reserved
dc.rights.uri
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectBinding Sitesen
dc.subjectCarrier Proteinsen
dc.subjectConserved Sequenceen
dc.subjectDrosophila Proteinsen
dc.subjectDrosophila melanogasteren
dc.subjectHumansen
dc.subjectMiceen
dc.subjectMolecular Sequence Dataen
dc.subjectPolyubiquitinen
dc.subjectProtein Bindingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Subunitsen
dc.subjectProtein Transporten
dc.subjectRatsen
dc.subjectUbiquitinationen
dc.titleUbiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBA-UBL polyubiquitin receptors.en
dc.typeArticle
prism.endingPage2470
prism.issueIdentifier12en
prism.publicationDate2012en
prism.publicationNameBiochemistryen
prism.startingPage2461
prism.volume51en
dc.identifier.doi10.17863/CAM.42171
dcterms.dateAccepted2012-02-27en
rioxxterms.versionofrecord10.1021/bi3001006en
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2012-03-27en
dc.identifier.eissn1520-4995
rioxxterms.typeJournal Article/Reviewen
cam.issuedOnline2012-02-27en
dc.identifier.urlhttps://pubs.acs.org/doi/10.1021/bi3001006en
rioxxterms.freetoread.startdate2013-03-15


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