Klopfenstein, Dieter R.

[["dc.bibliographiccitation.artnumber","7523"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Bodensiek, Kai"],["dc.contributor.author","Fakhri, Nikta"],["dc.contributor.author","von Roden, Kerstin"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Majoul, Irina"],["dc.contributor.author","Schmidt, Christoph"],["dc.contributor.author","Klopfenstein, Dieter R."],["dc.date.accessioned","2017-09-07T11:43:42Z"],["dc.date.available","2017-09-07T11:43:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Actin 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 alpha-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 alpha-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling."],["dc.identifier.doi","10.1038/ncomms8523"],["dc.identifier.gro","3141869"],["dc.identifier.isi","000358851600001"],["dc.identifier.pmid","26146072"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1978"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1161880"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Worm"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Klopfenstein, Dieter R."],["dc.contributor.author","Schmidt, Christoph"],["dc.date.accessioned","2017-09-07T11:54:10Z"],["dc.date.available","2017-09-07T11:54:10Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1080/21624054.2016.1161880"],["dc.identifier.gro","3145134"],["dc.identifier.pmid","27383012"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16933"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2837"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.publisher","Informa UK Limited"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/340528/EU//CELLMECHANOCONTROL"],["dc.relation.issn","2162-4054"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0/"],["dc.title","Game of Zones: how actin-binding proteins organize muscle contraction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","26965"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Haertig, Wolfgang"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Erck, Christian"],["dc.contributor.author","Grosche, Jens"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schmidt, Christoph"],["dc.contributor.author","Klopfenstein, Dieter R."],["dc.contributor.author","Chua, John Jia En"],["dc.date.accessioned","2017-09-07T11:44:53Z"],["dc.date.available","2017-09-07T11:44:53Z"],["dc.date.issued","2016"],["dc.description.abstract","Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer's disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration."],["dc.identifier.doi","10.1038/srep26965"],["dc.identifier.gro","3141678"],["dc.identifier.isi","000376866800001"],["dc.identifier.pmid","27247180"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8451"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]