Show simple item record

dc.contributor.authorNathan, James A
dc.contributor.authorSengupta, Soma
dc.contributor.authorWood, Stephen A
dc.contributor.authorAdmon, Arie
dc.contributor.authorMarkson, Gabriel
dc.contributor.authorSanderson, Chris
dc.contributor.authorLehner, Paul J
dc.contributor.editorFrances M Brodsky, Mark C P Marsh
dc.date.accessioned2017-05-03T16:58:20Z
dc.date.available2017-05-03T16:58:20Z
dc.date.issued2008
dc.date.modified2009-12-07T03:34:17Z
dc.identifier.issn1398-9219
dc.identifier.doi10.1111/j.1600-0854.2008.00747.x
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley-Blackwell Munksgaard
dc.publisher.placeDenmark
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom1130
dc.relation.ispartofpageto1145
dc.relation.ispartofissue7
dc.relation.ispartofjournalTraffic
dc.relation.ispartofvolume9
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode3207
dc.titleThe Ubiquitin E3 Ligase MARCH7 is Differentially Regulated by the Deubiquitylating Enzymes USP7 and USP9X
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2008
gro.hasfulltextNo Full Text
gro.griffith.authorWood, Stephen A.


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