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dc.contributor.authorXu, Zhuojinen_US
dc.contributor.authorXia, Binen_US
dc.contributor.authorGong, Qiangen_US
dc.contributor.authorBailey, Jeffreyen_US
dc.contributor.authorGroves, Benjaminen_US
dc.contributor.authorRadeke, Monteen_US
dc.contributor.authorWood, Stephenen_US
dc.contributor.authorK. Szumlinski, Karenen_US
dc.contributor.authorMa, Dzwokaien_US
dc.date.accessioned2017-05-03T13:50:45Z
dc.date.available2017-05-03T13:50:45Z
dc.date.issued2010en_US
dc.date.modified2011-03-07T08:55:52Z
dc.identifier.issn19326203en_US
dc.identifier.doi10.1371/journal.pone.0009725en_AU
dc.identifier.urihttp://hdl.handle.net/10072/36933
dc.description.abstractActivator of G protein Signaling 3 (AGS3) is a receptor-independent G protein activator that has been implicated in multiple biological events such as brain development, neuroplasticity and addiction, cardiac function, Golgi structure/function, macroautophagy and metabolism. However, how AGS3 is regulated is little known. We demonstrate here that AGS3 interacts with a ubiquitin specific protease USP9x, and this interaction is at least partially mediated through the C-terminal G protein regulatory domain of AGS3. Knockdown of USP9x causes a moderate reduction in the level of AGS3. In contrast, overexpression of either USP9x or its deubiquitinating domain UCH increases the amount of AGS3, whereas expression of the mutant UCH domain that lacks deubiquitinating activity does not have the same effect. As previously observed in AGS3 knockdown cells, the localization of several marker proteins of the late Golgi compartments is disturbed in cells depleted of USP9x. Taken together, our study suggests that USP9x can modulate the level of a subpopulation of AGS3, and this modulation plays a role in regulating the structure of the late Golgi compartments. Finally, we have found that levels of AGS3 and USP9x are co-regulated in the prefrontal cortex of rats withdrawn from repeated cocaine treatment. In conjunction with the above data, this observation indicates a potential role of USP9X in the regulation of the AGS3 level during cocaine-induced neuroplasticity.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.format.extent1400908 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherPublic Library of Scienceen_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrome9725-1en_US
dc.relation.ispartofpagetoe9725-12en_US
dc.relation.ispartofissue3en_US
dc.relation.ispartofjournalPloS Oneen_US
dc.relation.ispartofvolume5en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classifieden_US
dc.subject.fieldofresearchcode060199en_US
dc.titleIdentification of a Deubiquitinating Enzyme as a Novel AGS3-Interacting Proteinen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
dcterms.licensehttp://www.plos.org/journals/license.htmlen_US
gro.rights.copyrightCopyright 2010 Xu et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License CCAL. (http://www.plos.org/journals/license.html)en_AU
gro.date.issued2010
gro.hasfulltextFull Text


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