Dresbach, Thomas

[["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","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"]]