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dc.contributor.authorSchroder, WA
dc.contributor.authorBuck, M
dc.contributor.authorCloonan, N
dc.contributor.authorHancock, JF
dc.contributor.authorSuhrbier, A
dc.contributor.authorSculley, T
dc.contributor.authorBushell, G
dc.date.accessioned2017-05-03T11:32:22Z
dc.date.available2017-05-03T11:32:22Z
dc.date.issued2007
dc.date.modified2009-12-05T05:14:41Z
dc.identifier.issn0898-6568
dc.identifier.doi10.1016/j.cellsig.2007.01.013
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeUnited States
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/525462/description#description
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom1279
dc.relation.ispartofpageto1289
dc.relation.ispartofjournalCellular Signalling
dc.relation.ispartofvolume19
dc.rights.retentionY
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchMedical physiology
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3208
dc.titleHuman Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2007
gro.hasfulltextNo Full Text
gro.griffith.authorBushell, Gillian R.
gro.griffith.authorSchroder, Wayne


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