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dc.contributor.authorXavier, Charles-Peteren_US
dc.contributor.authorH. Rastetter, Raphaelen_US
dc.contributor.authorStumpf, Mariaen_US
dc.contributor.authorRosentreter, Andréen_US
dc.contributor.authorMüller, Rolfen_US
dc.contributor.authorReimann, Jensen_US
dc.contributor.authorCornfine, Susanneen_US
dc.contributor.authorLinder, Stefanen_US
dc.contributor.authorvan Vliet, Vanessaen_US
dc.contributor.authorHofmann, Andreasen_US
dc.contributor.authorO. Morgan, Reginalden_US
dc.contributor.authorFernandez, Maria-Pilaren_US
dc.contributor.authorSchröder, Rolfen_US
dc.contributor.authorA. Noegel, Angelikaen_US
dc.contributor.authorS. Clemen, Christophen_US
dc.date.accessioned2017-04-24T12:51:40Z
dc.date.available2017-04-24T12:51:40Z
dc.date.issued2009en_US
dc.date.modified2009-12-17T22:32:19Z
dc.identifier.issn0022-2836en_US
dc.identifier.doi10.1016/j.jmb.2009.07.079en_AU
dc.identifier.urihttp://hdl.handle.net/10072/27715
dc.description.abstractCoronin 1C (synonyms: coronin-3, CRN2), a WD40 repeat-containing protein involved in cellular actin dynamics, is ubiquitously expressed in human tissues. Here, we report on the identification and functional characterization of two novel coronin 1C isoforms, referred to as CRN2i2 and CRN2i3, which also associate with F-actin. Analyses of the coronin 1C gene disclosed a single promoter containing binding sites for myogenic regulatory factors and an alternative first exon 1b present in intron 1, which give rise to the novel isoforms. Chromatin immunoprecipitation studies demonstrate MyoD binding to a region of the CRN2 gene, which contains a highly conserved E-box element in exon 1a. Gel-filtration assays suggest that the largest isoform 3 exists as a monomer, in contrast to isoform 1 and isoform 2 appearing as trimers. CRN2i3, which can be induced by MyoD, is exclusively expressed in well-differentiated myoblasts as well as in mature skeletal muscle tissue. In human skeletal muscle, CRN2i3 is a novel component of postsynaptic neuromuscular junctions and thin filaments of myofibrils. Together, our findings postulate a role for CRN2 isoforms in the structural and functional organization of F-actin in highly ordered protein complexes.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.format.extent638708 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeNetherlandsen_US
dc.publisher.urihttp://www.elsevier.com/locate/jmben_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom287en_US
dc.relation.ispartofpageto299en_US
dc.relation.ispartofissue2en_US
dc.relation.ispartofjournalJournal of Molecular Biologyen_US
dc.relation.ispartofvolume393en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchAnalytical Biochemistryen_US
dc.subject.fieldofresearchcode060101en_US
dc.titleStructural and functional diversity of novel coronin 1C (CRN2) isoforms in muscleen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightCopyright 2009 Elsevier. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.en_AU
gro.date.issued2009
gro.hasfulltextFull Text


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