Show simple item record

dc.contributor.authorA. Nathan, Jamesen_US
dc.contributor.authorSengupta, Somaen_US
dc.contributor.authorA. Wood, Stephenen_US
dc.contributor.authorAdmon, Arieen_US
dc.contributor.authorMarkson, Gabrielen_US
dc.contributor.authorSanderson, Chrisen_US
dc.contributor.authorJ. Lehner, Paulen_US
dc.contributor.editorFrances M Brodsky, Mark C P Marshen_US
dc.date.accessioned2017-04-24T14:54:56Z
dc.date.available2017-04-24T14:54:56Z
dc.date.issued2008en_US
dc.date.modified2009-12-07T03:34:17Z
dc.identifier.issn13989219en_US
dc.identifier.doi10.1111/j.1600-0854.2008.00747.xen_AU
dc.identifier.urihttp://hdl.handle.net/10072/27123
dc.description.abstractProtein modification by one or more ubiquitin chains serves a critical signalling function across a wide range of cellular processes. Specificity within this system is conferred by ubiquitin E3 ligases, which target the substrates. Their activity is balanced by deubiquitylating enzymes (DUBs), which remove ubiquitin from both substrates and ligases. The RING-CH ligases were initially identified as viral immunoevasins involved in the downregulation of immunoreceptors. Their cellular orthologues, the Membrane-Associated RING-CH (MARCH) family represent a subgroup of the classical RING genes. Unlike their viral counterparts, the cellular RING-CH proteins appear highly regulated, and one of these in particular, MARCH7, was of interest because of a potential role in neuronal development and lymphocyte proliferation. Difficulties in detection and expression of this orphan ligase lead us to search for cellular cofactors involved in MARCH7 stability. In this study, we show that MARCH7 readily undergoes autoubiquitylation and associates with two deubiquitylating enzymes - ubiquitin-specific protease (USP)9X in the cytosol and USP7 in the nucleus. Exogenous expression and short interfering RNA depletion experiments demonstrate that MARCH7 can be stabilized by both USP9X and USP7, which deubiquitylate MARCH7 in the cytosol and nucleus, respectively. We therefore demonstrate compartment-specific regulation of this E3 ligase through recruitment of site-specific DUBs.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherWiley-Blackwell Munksgaarden_US
dc.publisher.placeDenmarken_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1130en_US
dc.relation.ispartofpageto1145en_US
dc.relation.ispartofissue7en_US
dc.relation.ispartofjournalTrafficen_US
dc.relation.ispartofvolume9en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classifieden_US
dc.subject.fieldofresearchcode060199en_US
dc.titleThe Ubiquitin E3 Ligase MARCH7 is Differentially Regulated by the Deubiquitylating Enzymes USP7 and USP9Xen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2008
gro.hasfulltextNo Full Text


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record