Klopfenstein, Dieter R.

[["dc.bibliographiccitation.firstpage","5862"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","5867"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Chua, John Jia En"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Worseck, Josephine M."],["dc.contributor.author","Kittelmann, Maike"],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Behrmann, Elmar"],["dc.contributor.author","Stelzl, Ulrich"],["dc.contributor.author","Pavlos, Nathan J."],["dc.contributor.author","Lalowski, Maciej M."],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Wanker, Erich E."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2018-11-07T09:11:12Z"],["dc.date.available","2018-11-07T09:11:12Z"],["dc.date.issued","2012"],["dc.description.abstract","Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases."],["dc.identifier.doi","10.1073/pnas.1113819109"],["dc.identifier.isi","000302533500062"],["dc.identifier.pmid","22451907"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26667"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Henschel, Volker"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Schmidt, Christoph F."],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.date.accessioned","2018-11-07T08:53:35Z"],["dc.date.available","2018-11-07T08:53:35Z"],["dc.date.issued","2011"],["dc.format.extent","150"],["dc.identifier.isi","000293637300385"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22451"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["dc.relation.issn","0175-7571"],["dc.title","Detecting protein conformational states in C. elegans in vivo by confocal fluorescence anisotropy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","19605"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","19610"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Wagner, Oliver"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Koehler, Barbara"],["dc.contributor.author","Chen, Chih-Wei"],["dc.contributor.author","Shen, Che-Piao"],["dc.contributor.author","Wu, Gong-Her"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Mandalapu, Sailaja"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.date.accessioned","2018-11-07T11:22:00Z"],["dc.date.available","2018-11-07T11:22:00Z"],["dc.date.issued","2009"],["dc.description.abstract","Kinesin-3 motor UNC-104/KIF1A is essential for transporting synaptic precursors to synapses. Although the mechanism of cargo binding is well understood, little is known how motor activity is regulated. We mapped functional interaction domains between SYD-2 and UNC-104 by using yeast 2-hybrid and pull-down assays and by using FRET/fluorescence lifetime imaging microscopy to image the binding of SYD-2 to UNC-104 in living Caenorhabditis elegans. We found that UNC-104 forms SYD-2-dependent axonal clusters (appearing during the transition from L2 to L3 larval stages), which behave in FRAP experiments as dynamic aggregates. High-resolution microscopy reveals that these clusters contain UNC-104 and synaptic precursors (synaptobrevin-1). Analysis of motor motility indicates bi-directional movement of UNC-104, whereas in syd-2 mutants, loss of SYD-2 binding reduces net anterograde movement and velocity (similar after deleting UNC-104's liprin-binding domain), switching to retrograde transport characteristics when no role of SYD-2 on dynein and conventional kinesin UNC-116 motility was found. These data present a kinesin scaffolding protein that controls both motor clustering along axons and motor motility, resulting in reduced cargo transport efficiency upon loss of interaction."],["dc.identifier.doi","10.1073/pnas.0902949106"],["dc.identifier.isi","000271907400068"],["dc.identifier.pmid","19880746"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55905"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Synaptic scaffolding protein SYD-2 clusters and activates kinesin-3 UNC-104 in C. elegans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]