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dc.contributor.authorP. Grou, Cláudiaen_US
dc.contributor.authorFrancisco, Tâniaen_US
dc.contributor.authorA. Rodrigues, Tonyen_US
dc.contributor.authorO. Freitas, Martaen_US
dc.contributor.authorP. Pinto, Manuelen_US
dc.contributor.authorF. Carvalho, Andreiaen_US
dc.contributor.authorDomingues, Pedroen_US
dc.contributor.authorWood, Stephenen_US
dc.contributor.authorE. Rodriguez-Borges, Joséen_US
dc.contributor.authorSa-Miranda, Claraen_US
dc.contributor.authorFransen, Marcen_US
dc.contributor.authorE. Azevedo, Jorgeen_US
dc.date.accessioned2017-04-24T13:00:45Z
dc.date.available2017-04-24T13:00:45Z
dc.date.issued2012en_US
dc.date.modified2012-09-21T04:17:29Z
dc.identifier.issn00219258en_US
dc.identifier.doi10.1074/jbc.M112.340158en_US
dc.identifier.urihttp://hdl.handle.net/10072/46986
dc.description.abstractPeroxin 5 (PEX5), the peroxisomal protein shuttling receptor, binds newly synthesized peroxisomal matrix proteins in the cytosol and promotes their translocation across the organelle membrane. During the translocation step, PEX5 itself becomes inserted into the peroxisomal docking/translocation machinery. PEX5 is then monoubiquitinated at a conserved cysteine residue and extracted back into the cytosol in an ATP-dependent manner. We have previously shown that the ubiquitin-PEX5 thioester conjugate (Ub-PEX5) released into the cytosol can be efficiently disrupted by physiological concentrations of glutathione, raising the possibility that a fraction of Ub-PEX5 is nonenzymatically deubiquitinated in vivo. However, data suggesting that Ub-PEX5 is also a target of a deubiquitinase were also obtained in that work. Here, we used an unbiased biochemical approach to identify this enzyme. Our results suggest that ubiquitin-specific protease 9X (USP9X) is by far the most active deubiquitinase acting on Ub-PEX5, both in female rat liver and HeLa cells. We also show that USP9X is an elongated monomeric protein with the capacity to hydrolyze thioester, isopeptide, and peptide bonds. The strategy described here will be useful in identifying deubiquitinases acting on other ubiquitin conjugates.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_US
dc.languageEnglishen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc.en_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_US
dc.relation.ispartofpagefrom12815en_US
dc.relation.ispartofpageto12827en_US
dc.relation.ispartofissue16en_US
dc.relation.ispartofjournalJournal of Biological Chemistryen_US
dc.relation.ispartofvolume287en_US
dc.rights.retentionYen_US
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classifieden_US
dc.subject.fieldofresearchcode060199en_US
dc.titleIdentification of Ubiquitin-specific Protease 9X (USP9X) as a Deubiquitinase Acting on Ubiquitin-Peroxin 5 (PEX5) Thioester Conjugateen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2012
gro.hasfulltextNo Full Text


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