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dc.contributor.authorXavier, Charles-Peter
dc.contributor.authorRastetter, Raphael H
dc.contributor.authorStumpf, Maria
dc.contributor.authorRosentreter, Andre
dc.contributor.authorMueller, Rolf
dc.contributor.authorReimann, Jens
dc.contributor.authorCornfine, Susanne
dc.contributor.authorLinder, Stefan
dc.contributor.authorvan Vliet, Vanessa
dc.contributor.authorHofmann, Andreas
dc.contributor.authorMorgan, Reginald O
dc.contributor.authorFernandez, Maria-Pilar
dc.contributor.authorSchroeder, Rolf
dc.contributor.authorNoegel, Angelika A
dc.contributor.authorClemen, Christoph S
dc.date.accessioned2017-05-03T15:19:43Z
dc.date.available2017-05-03T15:19:43Z
dc.date.issued2009
dc.date.modified2009-12-17T22:32:19Z
dc.identifier.issn0022-2836
dc.identifier.doi10.1016/j.jmb.2009.07.079
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent638708 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeNetherlands
dc.publisher.urihttp://www.elsevier.com/locate/jmb
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom287
dc.relation.ispartofpageto299
dc.relation.ispartofissue2
dc.relation.ispartofjournalJournal of Molecular Biology
dc.relation.ispartofvolume393
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchAnalytical biochemistry
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310101
dc.subject.fieldofresearchcode3107
dc.titleStructural and functional diversity of novel coronin 1C (CRN2) isoforms in muscle
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 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.
gro.date.issued2009
gro.hasfulltextFull Text
gro.griffith.authorHofmann, Andreas


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