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.artnumber","215"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","BMC Biology"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Petkova-Tuffy, Andonia"],["dc.contributor.author","Gödecke, Nina"],["dc.contributor.author","Viotti, Julio"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2021-11-25T11:00:09Z"],["dc.date.accessioned","2022-08-18T12:34:45Z"],["dc.date.available","2021-11-25T11:00:09Z"],["dc.date.available","2022-08-18T12:34:45Z"],["dc.date.issued","2021-09-27"],["dc.date.updated","2022-07-29T12:07:09Z"],["dc.description.abstract","Background Maturation is a process that allows synapses to acquire full functionality, optimizing their activity to diverse neural circuits, and defects in synaptic maturation may contribute to neurodevelopmental disorders. Neuroligin-1 (NL1) is a postsynaptic cell adhesion molecule essential for synapse maturation, a role typically attributed to binding to pre-synaptic ligands, the neurexins. However, the pathways underlying the action of NL1 in synaptic maturation are incompletely understood, and some of its previously observed effects seem reminiscent of those described for the neurotrophin brain-derived neurotrophic factor (BDNF). Here, we show that maturational increases in active zone stability and synaptic vesicle recycling rely on the joint action of NL1 and brain-derived neurotrophic factor (BDNF). Results Applying BDNF to hippocampal neurons in primary cultures or organotypical slice cultures mimicked the effects of overexpressing NL1 on both structural and functional maturation. Overexpressing a NL1 mutant deficient in neurexin binding still induced presynaptic maturation. Like NL1, BDNF increased synaptic vesicle recycling and the augmentation of transmitter release by phorbol esters, both hallmarks of presynaptic maturation. Mimicking the effects of NL1, BDNF also increased the half-life of the active zone marker bassoon at synapses, reflecting increased active zone stability. Overexpressing NL1 increased the expression and synaptic accumulation of BDNF. Inhibiting BDNF signaling pharmacologically or genetically prevented the effects of NL1 on presynaptic maturation. Applying BDNF to NL1-knockout mouse cultures rescued defective presynaptic maturation, indicating that BDNF acts downstream of NL1 and can restore presynaptic maturation at late stages of network development. Conclusions Our data introduce BDNF as a novel and essential component in a transsynaptic pathway linking NL1-mediated cell adhesion, neurotrophin action, and presynaptic maturation. Our findings connect synaptic cell adhesion and neurotrophin signaling and may provide a therapeutic approach to neurodevelopmental disorders by targeting synapse maturation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.citation","BMC Biology. 2021 Sep 27;19(1):215"],["dc.identifier.doi","10.1186/s12915-021-01145-7"],["dc.identifier.pii","1145"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/93518"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112933"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.publisher","BioMed Central"],["dc.relation.eissn","1741-7007"],["dc.rights","CC BY 4.0"],["dc.rights.holder","The Author(s)"],["dc.subject","Neuroligin-1,Brain-derived neurotrophic factor"],["dc.subject","Presynaptic maturation"],["dc.title","Neuroligin-1 mediates presynaptic maturation through brain-derived neurotrophic factor signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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.journal","Frontiers in Synaptic Neuroscience"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Viotti, Julio S."],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2020-12-10T18:44:35Z"],["dc.date.available","2020-12-10T18:44:35Z"],["dc.date.issued","2019"],["dc.description.abstract","Neurotransmitter release relies on an evolutionarily conserved presynaptic machinery. Nonetheless, some proteins occur in certain species and synapses, and are absent in others, indicating that they may have modulatory roles. How such proteins expand the power or versatility of the core release machinery is unclear. The presynaptic protein Mover/TPRGL/SVAP30 is heterogeneously expressed among synapses of the rodent brain, suggesting that it may add special functions to subtypes of presynaptic terminals. Mover is a synaptic vesicle-attached phosphoprotein that binds to Calmodulin and the active zone scaffolding protein Bassoon. Here we use a Mover knockout mouse line to investigate the role of Mover in the hippocampal mossy fiber (MF) to CA3 pyramidal cell synapse and Schaffer collateral to CA1. While Schaffer collateral synapses were unchanged by the knockout, the MFs showed strongly increased facilitation. The effect of Mover knockout in facilitation was both calcium- and age-dependent, having a stronger effect at higher calcium concentrations and in younger animals. Increasing cyclic adenosine monophosphate (cAMP) levels by forskolin equally potentiated both wildtype and knockout MF synapses, but occluded the increased facilitation observed in the knockout. These discoveries suggest that Mover has distinct roles at different synapses. At MF terminals, it acts to constrain the extent of presynaptic facilitation."],["dc.identifier.doi","10.3389/fnsyn.2019.00030"],["dc.identifier.eissn","1663-3563"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17148"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78516"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1663-3563"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Differential Effect on Hippocampal Synaptic Facilitation by the Presynaptic Protein Mover"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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","11116"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","11121"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Stan, A."],["dc.contributor.author","Pielarski, K. N."],["dc.contributor.author","Brigadski, T."],["dc.contributor.author","Wittenmayer, N."],["dc.contributor.author","Fedorchenko, O."],["dc.contributor.author","Gohla, A."],["dc.contributor.author","Lessmann, V."],["dc.contributor.author","Dresbach, T."],["dc.contributor.author","Gottmann, K."],["dc.date.accessioned","2019-07-09T11:52:58Z"],["dc.date.available","2019-07-09T11:52:58Z"],["dc.date.issued","2010"],["dc.description.abstract","Cell adhesion molecules are key players in transsynaptic communication, precisely coordinating presynaptic differentiation with postsynaptic specialization. At glutamatergic synapses, their retrograde signaling has been proposed to control presynaptic vesicle clustering at active zones. However, how the different types of cell adhesion molecules act together during this decisive step of synapse maturation is largely unexplored. Using a knockout approach, we show that two synaptic adhesion systems, N-cadherin and neuroligin-1, cooperate to control vesicle clustering at nascent synapses. Live cell imaging and fluorescence recovery after photobleaching experiments at individual synaptic boutons revealed a strong impairment of vesicle accumulation in the absence of N-cadherin, whereas the formation of active zones was largely unaffected. Strikingly, also the clustering of synaptic vesicles triggered by neuroligin-1 overexpression required the presence of N-cadherin in cultured neurons. Mechanistically, we found that N-cadherin acts by postsynaptically accumulating neuroligin-1 and activating its function via the scaffolding molecule S-SCAM, leading, in turn, to presynaptic vesicle clustering. A similar cooperation of N-cadherin and neuroligin-1 was observed in immature CA3 pyramidal neurons in an organotypic hippocampal network. Moreover, at mature synapses, N-cadherin was required for the increase in release probability and miniature EPSC frequency induced by expressed neuroligin-1. This cooperation of two cell adhesion systems provides a mechanism for coupling bidirectional synapse maturation mediated by neuroligin-1 to cell type recognition processes mediated by classical cadherins."],["dc.identifier.doi","10.1073/pnas.0914233107"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6249"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60310"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Ghelani, Tina"],["dc.contributor.author","Montenegro-Venegas, Carolina"],["dc.contributor.author","Fejtova, Anna"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2022-01-11T14:06:15Z"],["dc.date.available","2022-01-11T14:06:15Z"],["dc.date.issued","2021"],["dc.description.abstract","Bassoon is a core scaffold protein of the presynaptic active zone. In brain synapses, the C-terminus of Bassoon is oriented toward the plasma membrane and its N-terminus is oriented toward synaptic vesicles. At the Golgi-apparatus, Bassoon is thought to assemble active zone precursor structures, but whether it is arranged in an orderly fashion is unknown. Understanding the topology of this large scaffold protein is important for models of active zone biogenesis. Using stimulated emission depletion nanoscopy in cultured hippocampal neurons, we found that an N-terminal intramolecular tag of recombinant Bassoon, but not C-terminal tag, colocalized with markers of the trans- Golgi network (TGN). The N-terminus of Bassoon was located between 48 and 69 nm away from TGN38, while its C-terminus was located between 100 and 115 nm away from TGN38. Sequences within the first 95 amino acids of Bassoon were required for this arrangement. Our results indicate that, at the Golgi-apparatus, Bassoon is oriented with its N-terminus toward and its C-terminus away from the trans Golgi network membrane. Moreover, they suggest that Bassoon is an extended molecule at the trans Golgi network with the distance between amino acids 97 and 3,938, estimated to be between 46 and 52 nm. Our data are consistent with a model, in which the N-terminus of Bassoon binds to the membranes of the trans- Golgi network, while the C-terminus associates with active zone components, thus reflecting the topographic arrangement characteristic of synapses also at the Golgi-apparatus."],["dc.description.abstract","Bassoon is a core scaffold protein of the presynaptic active zone. In brain synapses, the C-terminus of Bassoon is oriented toward the plasma membrane and its N-terminus is oriented toward synaptic vesicles. At the Golgi-apparatus, Bassoon is thought to assemble active zone precursor structures, but whether it is arranged in an orderly fashion is unknown. Understanding the topology of this large scaffold protein is important for models of active zone biogenesis. Using stimulated emission depletion nanoscopy in cultured hippocampal neurons, we found that an N-terminal intramolecular tag of recombinant Bassoon, but not C-terminal tag, colocalized with markers of the trans- Golgi network (TGN). The N-terminus of Bassoon was located between 48 and 69 nm away from TGN38, while its C-terminus was located between 100 and 115 nm away from TGN38. Sequences within the first 95 amino acids of Bassoon were required for this arrangement. Our results indicate that, at the Golgi-apparatus, Bassoon is oriented with its N-terminus toward and its C-terminus away from the trans Golgi network membrane. Moreover, they suggest that Bassoon is an extended molecule at the trans Golgi network with the distance between amino acids 97 and 3,938, estimated to be between 46 and 52 nm. Our data are consistent with a model, in which the N-terminus of Bassoon binds to the membranes of the trans- Golgi network, while the C-terminus associates with active zone components, thus reflecting the topographic arrangement characteristic of synapses also at the Golgi-apparatus."],["dc.identifier.doi","10.3389/fnmol.2021.744034"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97864"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-507"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1662-5099"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Nanoscopical Analysis Reveals an Orderly Arrangement of the Presynaptic Scaffold Protein Bassoon at the Golgi-Apparatus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e63474"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Ahmed, Saheeb"],["dc.contributor.author","Wittenmayer, Nina"],["dc.contributor.author","Kremer, Thomas"],["dc.contributor.author","Hoeber, Jan"],["dc.contributor.author","Kiran Akula, Asha"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Islinger, Markus"],["dc.contributor.author","Kirsch, Joachim"],["dc.contributor.author","Dean, Camin"],["dc.contributor.author","Dresbach, Thomas"],["dc.contributor.editor","Dunaevsky, Anna"],["dc.date.accessioned","2018-09-28T09:31:14Z"],["dc.date.available","2018-09-28T09:31:14Z"],["dc.date.issued","2013"],["dc.description.abstract","With remarkably few exceptions, the molecules mediating synaptic vesicle exocytosis at active zones are structurally and functionally conserved between vertebrates and invertebrates. Mover was found in a yeast-2-hybrid assay using the vertebrate-specific active zone scaffolding protein bassoon as a bait. Peptides of Mover have been reported in proteomics screens for self-interacting proteins, phosphorylated proteins, and synaptic vesicle proteins, respectively. Here, we tested the predictions arising from these screens. Using flotation assays, carbonate stripping of peripheral membrane proteins, mass spectrometry, immunogold labelling of purified synaptic vesicles, and immuno-organelle isolation, we found that Mover is indeed a peripheral synaptic vesicle membrane protein. In addition, by generating an antibody against phosphorylated Mover and Western blot analysis of fractionated rat brain, we found that Mover is a bona fide phospho-protein. The localization of Mover to synaptic vesicles is phosphorylation dependent; treatment with a phosphatase caused Mover to dissociate from synaptic vesicles. A yeast-2-hybrid screen, co-immunoprecipitation and cell-based optical assays of homomerization revealed that Mover undergoes homophilic interaction, and regions within both the N- and C- terminus of the protein are required for this interaction. Deleting a region required for homomeric interaction abolished presynaptic targeting of recombinant Mover in cultured neurons. Together, these data prove that Mover is associated with synaptic vesicles, and implicate phosphorylation and multimerization in targeting of Mover to synaptic vesicles and presynaptic sites."],["dc.identifier.doi","10.1371/journal.pone.0063474"],["dc.identifier.pmid","23723986"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9347"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15843"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Mover is a homomeric phospho-protein present on synaptic vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Akula, Asha Kiran"],["dc.contributor.author","Zhang, Xin"],["dc.contributor.author","Viotti, Julio S."],["dc.contributor.author","Nestvogel, Dennis"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Ebrecht, Rene"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Wouters, Fred"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Bogeski, Ivan"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2020-12-10T18:44:35Z"],["dc.date.available","2020-12-10T18:44:35Z"],["dc.date.issued","2019"],["dc.description.abstract","Neurotransmitter release is mediated by an evolutionarily conserved machinery. The synaptic vesicle (SV) associated protein Mover/TPRGL/SVAP30 does not occur in all species and all synapses. Little is known about its molecular properties and how it may interact with the conserved components of the presynaptic machinery. Here, we show by deletion analysis that regions required for homomeric interaction of Mover are distributed across the entire molecule, including N-terminal, central and C-terminal regions. The same regions are also required for the accumulation of Mover in presynaptic terminals of cultured neurons. Mutating two phosphorylation sites in N-terminal regions did not affect these properties. In contrast, a point mutation in the predicted Calmodulin (CaM) binding sequence of Mover abolished both homomeric interaction and presynaptic targeting. We show that this sequence indeed binds Calmodulin, and that recombinant Mover increases Calmodulin signaling upon heterologous expression. Our data suggest that presynaptic accumulation of Mover requires homomeric interaction mediated by regions distributed across large areas of the protein, and corroborate the hypothesis that Mover functionally interacts with Calmodulin signaling."],["dc.identifier.doi","10.3389/fnmol.2019.00249"],["dc.identifier.eissn","1662-5099"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78512"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1662-5099"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The Calmodulin Binding Region of the Synaptic Vesicle Protein Mover Is Required for Homomeric Interaction and Presynaptic Targeting"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","15791"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Riemann, Donatus"],["dc.contributor.author","Wallrafen, Rebecca"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2018-10-10T08:59:42Z"],["dc.date.available","2018-10-10T08:59:42Z"],["dc.date.issued","2017-11-17"],["dc.description.abstract","Mutations in the human homolog of the Drosophila gene Rogdi cause Kohlschütter-Tönz syndrome. This disorder is characterised by amelogenesis imperfecta, as well as severe neurological symptoms including epilepsy and psychomotor delay. However, little is known about the protein encoded by Rogdi, and hence the pathogenic mechanisms underlying Kohlschütter-Tönz syndrome have remained elusive. Using immunofluorescence of rat cultured hippocampal neurons and brain sections we find that Rogdi is enriched at synaptic sites. In addition, recombinant GFP-Rogdi expressed in cultured neurons was efficiently targeted to presynaptic sites, where it colocalised with the presynaptic scaffolding protein Bassoon and the synaptic vesicle markers Synaptophysin, Synapsin-1, VAMP2/Synaptobrevin and Mover. Our data indicate that GFP-Rogdi harbours efficient signals for presynaptic targeting, and that Rogdi is a presynaptic protein. Thus, the neurological symptoms associated with Kohlschütter-Tönz syndrome may arise from presynaptic dysfunction."],["dc.fs.pkfprnr","69207"],["dc.identifier.doi","10.1038/s41598-017-16004-1"],["dc.identifier.fs","633270"],["dc.identifier.pmid","29150638"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14859"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15926"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2045-2322"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The Kohlschütter-Tönz syndrome associated gene Rogdi encodes a novel presynaptic protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]