Dresbach, Thomas

[["dc.bibliographiccitation.issue","143"],["dc.bibliographiccitation.journal","Journal of Visualized Experiments"],["dc.contributor.author","Wallrafen, Rebecca"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Viotti, Julio S."],["dc.date.accessioned","2020-12-10T18:47:30Z"],["dc.date.available","2020-12-10T18:47:30Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3791/58940"],["dc.identifier.eissn","1940-087X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78785"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Quantifying the Heterogeneous Distribution of a Synaptic Protein in the Mouse Brain Using Immunofluorescence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","136"],["dc.bibliographiccitation.journal","Journal of Visualized Experiments"],["dc.contributor.author","Riemann, Donatus"],["dc.contributor.author","Petkova, Andoniya"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Wallrafen, Rebecca"],["dc.date.accessioned","2020-12-10T18:47:29Z"],["dc.date.available","2020-12-10T18:47:29Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.3791/58043"],["dc.identifier.eissn","1940-087X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78783"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular and Cellular Neuroscience"],["dc.bibliographiccitation.lastpage","235"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Neeb, Antje"],["dc.contributor.author","Meyer, Guido"],["dc.contributor.author","Gundelfinger, Eckart D."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:43:09Z"],["dc.date.available","2017-09-07T11:43:09Z"],["dc.date.issued","2004"],["dc.description.abstract","Synaptic cell adhesion and synaptogenesis are thought to involve the interaction of neuroligin, a postsynaptic transmembrane protein, with its presynaptic ligand neurexin. Neuroligin also interacts with SAP90/ PSD95, a multidomain scaffolding protein thought to recruit proteins to postsynaptic sites. Using expression of GFP-tagged versions of neuroligin in cultured hippocampal neurons, we find that neuroligin is targeted to synapses via intracellular sequences distinct from its SAP90/PSD95 binding site. A neuroligin mutant lacking the intracellular domain fails to target to synapses. These data indicate that postsynaptic targeting of neuroligin does not rely on the scaffolding action of SAP90/PSD95 and is not induced by binding to presynaptic neurexin. Neuroligin is rather targeted to synapses via a postsynaptic mechanism, which may precede and be necessary for subsequent recruitment of neurexin and other neuroligin interactors such as SAP90/PSD95, suggesting a pivotal position for neuroligin in a putative hierarchy of interactions assembling or stabilizing synapses. (C) 2004 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.mcn.2004.06.013"],["dc.identifier.gro","3143935"],["dc.identifier.isi","000224950000002"],["dc.identifier.pmid","15519238"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1504"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1044-7431"],["dc.title","Synaptic targeting of neuroligin is independent of neurexin and SAP90/PSD95 binding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","669"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","680"],["dc.bibliographiccitation.volume","169"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Wegmeyer, Heike"],["dc.contributor.author","Brandstaetter, Johann Helmut"],["dc.contributor.author","Xue, Mingshan"],["dc.contributor.author","Rosenmund, C."],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Hofmann, K"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:54:25Z"],["dc.date.available","2017-09-07T11:54:25Z"],["dc.date.issued","2005"],["dc.description.abstract","Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH- terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH- terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons."],["dc.identifier.doi","10.1083/jcb.200502115"],["dc.identifier.gro","3143845"],["dc.identifier.isi","000229305400015"],["dc.identifier.pmid","15911881"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1404"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9525"],["dc.title","Structurally and functionally unique complexins at retinal ribbon synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","512"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","527"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Schulz, Alejandro Mendoza"],["dc.contributor.author","Jing, Zhizi"],["dc.contributor.author","Caro, Juan Maria Sanchez"],["dc.contributor.author","Wetzel, Friederike"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:46:28Z"],["dc.date.available","2017-09-07T11:46:28Z"],["dc.date.issued","2014"],["dc.description.abstract","Endbulb of Held terminals of auditory nerve fibers (ANF) transmit auditory information at hundreds per second to bushy cells (BCs) in the anteroventral cochlear nucleus (AVCN). Here, we studied the structure and function of endbulb synapses in mice that lack the presynaptic scaffold bassoon and exhibit reduced ANF input into the AVCN. Endbulb terminals and active zones were normal in number and vesicle complement. Postsynaptic densities, quantal size and vesicular release probability were increased while vesicle replenishment and the standing pool of readily releasable vesicles were reduced. These opposing effects canceled each other out for the first evoked EPSC, which showed unaltered amplitude. We propose that ANF activity deprivation drives homeostatic plasticity in the AVCN involving synaptic upscaling and increased intrinsic BC excitability. In vivo recordings from individual mutant BCs demonstrated a slightly improved response at sound onset compared to ANF, likely reflecting the combined effects of ANF convergence and homeostatic plasticity. Further, we conclude that bassoon promotes vesicular replenishment and, consequently, a large standing pool of readily releasable synaptic vesicles at the endbulb synapse."],["dc.identifier.doi","10.1002/embj.201385887"],["dc.identifier.gro","3142175"],["dc.identifier.isi","000332391600012"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5366"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Bassoon-disruption slows vesicle replenishment and induces homeostatic plasticity at a CNS synapse"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","204"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Neuroforum"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Wittenmayer, Nina"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2018-11-07T09:10:04Z"],["dc.date.available","2018-11-07T09:10:04Z"],["dc.date.issued","2012"],["dc.description.abstract","Synapse assembly is the cellular mechanism that mediates the generation of physical connections between nerve cells and, thus, allows for the establishment of functional connectivity in the brain. The biogenesis of a synapse requires a set of highly coordinated molecular events, ranging from initial formation of adhesive contacts between an axon and a dendrite, followed by the recruitment and precise arrangement of synaptic organelles and proteins on both sides of the synaptic cleft, and culminating in the maintenance and remodelling of the exquisite architecture of a differentiated, i.e. mature, synaptic junction. Both the postsynaptic and the presynaptic compartment are thought to undergo stages of maturation that change and shape synaptic structure and function in a characteristic way. Recent evidence suggests that transsynaptic signalling, elicited by postsynaptic cell adhesion molecules, regulates the molecular events underlying presynaptic maturation. Thus, synaptic cell adhesion molecules, apart from physically connecting nerve cells, emerge as coordinators of presynaptic and postsynaptic differentiation across the synaptic cleft."],["dc.identifier.isi","000321725700002"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26411"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Spektrum Akademischer Verlag-springer-verlag Gmbh"],["dc.relation.issn","0947-0875"],["dc.title","Structural and functional maturation of presynaptic nerve endings under control of transsynaptic signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","521"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","533"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Körber, Christoph"],["dc.contributor.author","Horstmann, Heinz"],["dc.contributor.author","Venkataramani, Varun"],["dc.contributor.author","Herrmannsdörfer, Frank"],["dc.contributor.author","Kremer, Thomas"],["dc.contributor.author","Kaiser, Michaela"],["dc.contributor.author","Schwenger, Darius B."],["dc.contributor.author","Ahmed, Saheeb"],["dc.contributor.author","Dean, Camin"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.author","Kuner, Thomas"],["dc.date.accessioned","2018-09-28T09:27:35Z"],["dc.date.available","2018-09-28T09:27:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Mover, a member of the exquisitely small group of vertebrate-specific presynaptic proteins, has been discovered as an interaction partner of the scaffolding protein Bassoon, yet its function has not been elucidated. We used adeno-associated virus (AAV)-mediated shRNA expression to knock down Mover in the calyx of Held in vivo. Although spontaneous synaptic transmission remained unaffected, we found a strong increase of the evoked EPSC amplitude. The size of the readily releasable pool was unaltered, but short-term depression was accelerated and enhanced, consistent with an increase in release probability after Mover knockdown. This increase in release probability was not caused by alterations in Ca(2+) influx but rather by a higher Ca(2+) sensitivity of the release machinery, as demonstrated by presynaptic Ca(2+) uncaging. We therefore conclude that Mover expression in certain subsets of synapses negatively regulates synaptic release probability, constituting a novel mechanism to tune synaptic transmission."],["dc.identifier.doi","10.1016/j.neuron.2015.07.001"],["dc.identifier.pmid","26212709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15842"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1097-4199"],["dc.title","Modulation of Presynaptic Release Probability by the Vertebrate-Specific Protein Mover"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13564"],["dc.bibliographiccitation.issue","32"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13569"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Wittenmayer, Nina"],["dc.contributor.author","Koerber, Christoph"],["dc.contributor.author","Liu, Huisheng"],["dc.contributor.author","Kremer, Thomas"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Chapman, Edwin R."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Kuner, Thomas"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2017-09-07T11:46:51Z"],["dc.date.available","2017-09-07T11:46:51Z"],["dc.date.issued","2009"],["dc.description.abstract","Presynaptic nerve terminals pass through distinct stages of maturation after their initial assembly. Here we show that the postsynaptic cell adhesion molecule Neuroligin1 regulates key steps of presynaptic maturation. Presynaptic terminals from Neuroligin1-knockout mice remain structurally and functionally immature with respect to active zone stability and synaptic vesicle pool size, as analyzed in cultured hippocampal neurons. Conversely, overexpression of Neuroligin1 in immature neurons, that is within the first 5 days after plating, induced the formation of presynaptic boutons that had hallmarks of mature boutons. In particular, Neuroligin1 enhanced the size of the pool of recycling synaptic vesicles, the rate of synaptic vesicle exocytosis, the fraction of boutons responding to depolarization, as well as the responsiveness of the presynaptic release machinery to phorbol ester stimulation. Moreover, Neuroligin1 induced the formation of active zones that remained stable in the absence of F-actin, another hallmark of advanced maturation. Acquisition of F-actin independence of the active zone marker Bassoon during culture development or induced via overexpression of Neuroligin1 was activity-dependent. The extracellular domain of Neuroligin1 was sufficient to induce assembly of functional presynaptic terminals, while the intracellular domain was required for terminal maturation. These data show that induction of presynaptic terminal assembly and maturation involve mechanistically distinct actions of Neuroligins, and that Neuroligin1 is essential for presynaptic terminal maturation."],["dc.identifier.doi","10.1073/pnas.0905819106"],["dc.identifier.gro","3143076"],["dc.identifier.isi","000268877300075"],["dc.identifier.pmid","19628693"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/550"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [DR 373/3-2, DR 373/3-3]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Postsynaptic Neuroligin1 regulates presynaptic maturation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]