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dc.contributor.authorGrou, Claudia P
dc.contributor.authorFrancisco, Tania
dc.contributor.authorRodrigues, Tony A
dc.contributor.authorFreitas, Marta O
dc.contributor.authorPinto, Manuel P
dc.contributor.authorCarvalho, Andreia F
dc.contributor.authorDomingues, Pedro
dc.contributor.authorWood, Stephen A
dc.contributor.authorRodriguez-Borges, Jose E
dc.contributor.authorSa-Miranda, Clara
dc.contributor.authorFransen, Marc
dc.contributor.authorAzevedo, Jorge E
dc.date.accessioned2018-03-20T12:31:13Z
dc.date.available2018-03-20T12:31:13Z
dc.date.issued2012
dc.date.modified2012-09-21T04:17:29Z
dc.identifier.issn1083-351X
dc.identifier.doi10.1074/jbc.M112.340158
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc.
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom12815
dc.relation.ispartofpageto12827
dc.relation.ispartofissue16
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume287
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.subject.fieldofresearchcode03
dc.titleIdentification of Ubiquitin-specific Protease 9X (USP9X) as a Deubiquitinase Acting on Ubiquitin-Peroxin 5 (PEX5) Thioester Conjugate
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2012
gro.hasfulltextNo Full Text
gro.griffith.authorWood, Stephen A.


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