ERBIN is a new SARA-interacting protein: competition between SARA and SMAD2 and SMAD3 for binding to ERBIN

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dc.contributor.authorSflomos, G.en
dc.contributor.authorKostaras, E.en
dc.contributor.authorPanopoulou, E.en
dc.contributor.authorPappas, N.en
dc.contributor.authorKyrkou, A.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorFotsis, T.en
dc.contributor.authorMurphy, C.en
dc.date.accessioned2015-11-24T19:18:40Z
dc.date.available2015-11-24T19:18:40Z
dc.identifier.issn1477-9137-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21886
dc.rightsDefault Licence-
dc.subjectActivins/metabolismen
dc.subjectAdaptor Proteins, Signal Transducing/chemistry/genetics/*metabolismen
dc.subjectAnimalsen
dc.subjectCell Lineen
dc.subjectCell Nucleus/metabolismen
dc.subjectGenes, Reporteren
dc.subjectHumansen
dc.subjectIntracellular Signaling Peptides and Proteins/chemistry/genetics/*metabolismen
dc.subjectLuciferases, Renilla/biosynthesis/geneticsen
dc.subjectMiceen
dc.subjectPeptide Fragments/metabolismen
dc.subjectProtein Bindingen
dc.subjectProtein Interaction Domains and Motifsen
dc.subjectProtein Transporten
dc.subjectRNA Interferenceen
dc.subjectResponse Elementsen
dc.subjectSerine Endopeptidases/chemistry/genetics/*metabolismen
dc.subjectSmad2 Protein/*metabolismen
dc.subjectSmad3 Protein/*metabolismen
dc.subjectTranscriptional Activationen
dc.subjectTransforming Growth Factor beta/metabolismen
dc.titleERBIN is a new SARA-interacting protein: competition between SARA and SMAD2 and SMAD3 for binding to ERBINen
heal.abstractSARA, an early endosomal protein, plays a key role in TGFbeta signalling, as it presents SMAD2 and SMAD3 for phosphorylation by the activated TGFbeta receptors. Here, we show that ERBIN is a new SARA-interacting protein that can be recruited by SARA to early endosomes. ERBIN was recently shown to bind and segregate phosphorylated SMAD2 and SMAD3 (SMAD2/3) in the cytoplasm, thereby inhibiting SMAD2/3-dependent transcription. SARA binds to ERBIN using a new domain, which we have called the ERBID (ERBIN-binding domain), whereas ERBIN binds to SARA using a domain (amino acids 1208-1265) that also interacts with SMAD2 and SMAD3, which we have called the SSID (SARA- and SMAD-interacting domain). We additionally show that SARA competes with SMAD2/3 for binding to ERBIN. In agreement, overexpression of SARA or the ERBID peptide reverses the inhibitory effect of ERBIN on SMAD2/3-dependent transcription. Taken together, these data suggest that the response of cells to TGFbeta and activin A can be influenced by the relative concentrations of SARA, ERBIN and SMAD2/3.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1242/jcs.062307-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/21878490-
heal.identifier.secondaryhttp://jcs.biologists.org/content/124/19/3209-
heal.journalNameJ Cell Scien
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2011-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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