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Klopfenstein, Dieter R.
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Klopfenstein, Dieter R.
Official Name
Klopfenstein, Dieter R.
Alternative Name
Klopfenstein, D.
Klopfenstein, D. R.
Klopfenstein, Dieter
Klopfenstein, Dieter Robert
Main Affiliation
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2012Journal Article [["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"]]Details DOI PMID PMC WOS2011Conference Abstract [["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"]]Details WOS2009Journal Article [["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"]]Details DOI PMID PMC WOS