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Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

dc.contributor.authorButkevich, Eugenia
dc.contributor.authorBodensiek, Kai
dc.contributor.authorFakhri, Nikta
dc.contributor.authorvon Roden, Kerstin
dc.contributor.authorSchaap, Iwan A. T.
dc.contributor.authorMajoul, Irina
dc.contributor.authorSchmidt, Christoph F.
dc.contributor.authorKlopfenstein, Dieter R.
dc.date.accessioned2019-12-16T11:38:33Z
dc.date.available2019-12-16T11:38:33Z
dc.date.issued2015de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/16945
dc.description.abstractActin filament organization and stability in the sarcomeres of muscle cells are critical for force generation. Here we identify and functionally characterize a Caenorhabditis elegans drebrin-like protein DBN-1 as a novel constituent of the muscle contraction machinery. In vitro, DBN-1 exhibits actin filament binding and bundling activity. In vivo, DBN-1 is expressed in body wall muscles of C. elegans. During the muscle contraction cycle, DBN-1 alternates location between myosin- and actin-rich regions of the sarcomere. In contracted muscle, DBN-1 is accumulated at I-bands where it likely regulates proper spacing of α-actinin and tropomyosin and protects actin filaments from the interaction with ADF/cofilin. DBN-1 loss of function results in the partial depolymerization of F-actin during muscle contraction. Taken together, our data show that DBN-1 organizes the muscle contractile apparatus maintaining the spatial relationship between actin-binding proteins such as α-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling.de
dc.language.isoengde
dc.rightsopenAccess
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectActin; Cell signalling; Muscle contractionde
dc.subject.ddc530
dc.titleDrebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contractionde
dc.typejournalArticlede
dc.identifier.doi10.1038/ncomms8523
dc.type.versionpublishedVersionde
dc.relation.eISSN2041-1723
dc.bibliographicCitation.volume6de
dc.bibliographicCitation.issue1de
dc.type.subtypejournalArticle
dc.bibliographicCitation.articlenumber7523de
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalNature Communicationsde


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