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dc.contributor.authorSchroder, Wayneen_US
dc.contributor.authorBuck, Marionen_US
dc.contributor.authorCloonan, Nicoleen_US
dc.contributor.authorF. Hancock, Johnen_US
dc.contributor.authorSuhrbier, Andreasen_US
dc.contributor.authorSculley, Tomen_US
dc.contributor.authorBushell, Gillianen_US
dc.date.accessioned2017-04-24T08:26:26Z
dc.date.available2017-04-24T08:26:26Z
dc.date.issued2007en_US
dc.date.modified2009-12-05T05:14:41Z
dc.identifier.issn08986568en_US
dc.identifier.doi10.1016/j.cellsig.2007.01.013en_AU
dc.identifier.urihttp://hdl.handle.net/10072/17399
dc.description.abstractHuman Sin1 (SAPK-interacting protein 1) is a member of a conserved family of orthologous proteins that have an essential role in signal transduction in yeast and Dictyostelium. This study demonstrates that most Sin1 orthologues contain both a Raf-like Ras-binding domain (RBD) and a pleckstrin homology (PH) domain. These domains are functional in the human Sin1 protein, with the PH domain involved in lipid and membrane binding by Sin1, and the RBD able to bind activated H-and K-Ras. Sin1 and Ras co-immunoprecipitated and co-localised, showing that these proteins associate with each other in vivo. Overexpression of Sin1 inhibited the activation of ERK, Akt and JNK signalling pathways by Ras. In contrast, siRNA knockdown of endogenous Sin1 protein expression in HEK293 cells enhanced the activation of ERK1/2 by Ras. These data suggest that Sin1 is a mammalian Ras-inhibitor.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevier Inc.en_US
dc.publisher.placeUnited Statesen_US
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/525462/description#descriptionen_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1279en_US
dc.relation.ispartofpageto1289en_US
dc.relation.ispartofjournalCellular Signallingen_US
dc.relation.ispartofvolume19en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode270103en_US
dc.titleHuman Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signallingen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2007
gro.hasfulltextNo Full Text


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