Wichmann, Carolin

[["dc.bibliographiccitation.firstpage","843"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","855"],["dc.bibliographiccitation.volume","177"],["dc.contributor.author","Besse, Florence"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Kittel, Robert J."],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Rasse, Tobias M."],["dc.contributor.author","Sigrist, Stephan J."],["dc.contributor.author","Ephrussi, Anne"],["dc.date.accessioned","2022-03-01T11:46:32Z"],["dc.date.available","2022-03-01T11:46:32Z"],["dc.date.issued","2007"],["dc.description.abstract","Synapses can undergo rapid changes in size as well as in their vesicle release function during both plasticity processes and development. This fundamental property of neuronal cells requires the coordinated rearrangement of synaptic membranes and their associated cytoskeleton, yet remarkably little is known of how this coupling is achieved. In a GFP exon-trap screen, we identified Drosophila melanogaster Basigin (Bsg) as an immunoglobulin domain-containing transmembrane protein accumulating at periactive zones of neuromuscular junctions. Bsg is required pre- and postsynaptically to restrict synaptic bouton size, its juxtamembrane cytoplasmic residues being important for that function. Bsg controls different aspects of synaptic structure, including distribution of synaptic vesicles and organization of the presynaptic cortical actin cytoskeleton. Strikingly, bsg function is also required specifically within the presynaptic terminal to inhibit nonsynchronized evoked vesicle release. We thus propose that Bsg is part of a transsynaptic complex regulating synaptic compartmentalization and strength, and coordinating plasma membrane and cortical organization."],["dc.description.abstract","Synapses can undergo rapid changes in size as well as in their vesicle release function during both plasticity processes and development. This fundamental property of neuronal cells requires the coordinated rearrangement of synaptic membranes and their associated cytoskeleton, yet remarkably little is known of how this coupling is achieved. In a GFP exon-trap screen, we identified Drosophila melanogaster Basigin (Bsg) as an immunoglobulin domain-containing transmembrane protein accumulating at periactive zones of neuromuscular junctions. Bsg is required pre- and postsynaptically to restrict synaptic bouton size, its juxtamembrane cytoplasmic residues being important for that function. Bsg controls different aspects of synaptic structure, including distribution of synaptic vesicles and organization of the presynaptic cortical actin cytoskeleton. Strikingly, bsg function is also required specifically within the presynaptic terminal to inhibit nonsynchronized evoked vesicle release. We thus propose that Bsg is part of a transsynaptic complex regulating synaptic compartmentalization and strength, and coordinating plasma membrane and cortical organization."],["dc.identifier.doi","10.1083/jcb.200701111"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103706"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","The Ig cell adhesion molecule Basigin controls compartmentalization and vesicle release at Drosophila melanogaster synapses"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1565"],["dc.bibliographiccitation.issue","6062"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1569"],["dc.bibliographiccitation.volume","334"],["dc.contributor.author","Liu, Karen S. Y."],["dc.contributor.author","Siebert, Matthias"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Knoche, Elena"],["dc.contributor.author","Wegener, Stephanie"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Matkovic, Tanja"],["dc.contributor.author","Muhammad, Karzan"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Mettke, Christoph"],["dc.contributor.author","Bueckers, Johanna"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Mueller, Martin"],["dc.contributor.author","Davis, Graeme W."],["dc.contributor.author","Schmitz, Dietmar"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2017-09-07T11:43:13Z"],["dc.date.available","2017-09-07T11:43:13Z"],["dc.date.issued","2011"],["dc.description.abstract","The molecular machinery mediating the fusion of synaptic vesicles (SVs) at presynaptic active zone (AZ) membranes has been studied in detail, and several essential components have been identified. AZ-associated protein scaffolds are viewed as only modulatory for transmission. We discovered that Drosophila Rab3-interacting molecule (RIM)-binding protein (DRBP) is essential not only for the integrity of the AZ scaffold but also for exocytotic neurotransmitter release. Two-color stimulated emission depletion microscopy showed that DRBP surrounds the central Ca(2+) channel field. In drbp mutants, Ca(2+) channel clustering and Ca(2+) influx were impaired, and synaptic release probability was drastically reduced. Our data identify RBP family proteins as prime effectors of the AZ scaffold that are essential for the coupling of SVs, Ca(2+) channels, and the SV fusion machinery."],["dc.identifier.doi","10.1126/science.1212991"],["dc.identifier.gro","3142613"],["dc.identifier.isi","000298091400056"],["dc.identifier.pmid","22174254"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0036-8075"],["dc.title","RIM-Binding Protein, a Central Part of the Active Zone, Is Essential for Neurotransmitter Release"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","The Journal of Physiological Sciences"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Kittel, Robert Johannes"],["dc.contributor.author","Hallermann, Stefan"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Dyba, Marcus"],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Sigrist, Stephan J."],["dc.contributor.author","Heckmann, Manfred"],["dc.date.accessioned","2018-11-07T08:34:56Z"],["dc.date.available","2018-11-07T08:34:56Z"],["dc.date.issued","2009"],["dc.format.extent","141"],["dc.identifier.isi","000271023100747"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17941"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Tokyo"],["dc.relation.issn","1880-6546"],["dc.title","The C-Terminal Domain of Bruchpilot Accelerates Vesicle Supply at Active Zones"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","129"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","145"],["dc.bibliographiccitation.volume","186"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Dyba, Marcus"],["dc.contributor.author","Hallermann, Stefan"],["dc.contributor.author","Kittel, Robert J."],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2022-03-01T11:46:32Z"],["dc.date.available","2022-03-01T11:46:32Z"],["dc.date.issued","2009"],["dc.description.abstract","Synaptic vesicles fuse at active zone (AZ) membranes where Ca2+ channels are clustered and that are typically decorated by electron-dense projections. Recently, mutants of the Drosophila melanogaster ERC/CAST family protein Bruchpilot (BRP) were shown to lack dense projections (T-bars) and to suffer from Ca2+ channel–clustering defects. In this study, we used high resolution light microscopy, electron microscopy, and intravital imaging to analyze the function of BRP in AZ assembly. Consistent with truncated BRP variants forming shortened T-bars, we identify BRP as a direct T-bar component at the AZ center with its N terminus closer to the AZ membrane than its C terminus. In contrast, Drosophila Liprin-α, another AZ-organizing protein, precedes BRP during the assembly of newly forming AZs by several hours and surrounds the AZ center in few discrete punctae. BRP seems responsible for effectively clustering Ca2+ channels beneath the T-bar density late in a protracted AZ formation process, potentially through a direct molecular interaction with intracellular Ca2+ channel domains."],["dc.description.abstract","Synaptic vesicles fuse at active zone (AZ) membranes where Ca2+ channels are clustered and that are typically decorated by electron-dense projections. Recently, mutants of the Drosophila melanogaster ERC/CAST family protein Bruchpilot (BRP) were shown to lack dense projections (T-bars) and to suffer from Ca2+ channel–clustering defects. In this study, we used high resolution light microscopy, electron microscopy, and intravital imaging to analyze the function of BRP in AZ assembly. Consistent with truncated BRP variants forming shortened T-bars, we identify BRP as a direct T-bar component at the AZ center with its N terminus closer to the AZ membrane than its C terminus. In contrast, Drosophila Liprin-α, another AZ-organizing protein, precedes BRP during the assembly of newly forming AZs by several hours and surrounds the AZ center in few discrete punctae. BRP seems responsible for effectively clustering Ca2+ channels beneath the T-bar density late in a protracted AZ formation process, potentially through a direct molecular interaction with intracellular Ca2+ channel domains."],["dc.identifier.doi","10.1083/jcb.200812150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103707"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Maturation of active zone assembly by Drosophila Bruchpilot"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1219"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Neuroscience"],["dc.bibliographiccitation.lastpage","1226"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Khorramshahi, Omid"],["dc.contributor.author","Gupta, Varun K"],["dc.contributor.author","Banovic, Daniel"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Reynolds, Eric"],["dc.contributor.author","Sigrist, Stephan J"],["dc.date.accessioned","2022-03-01T11:45:54Z"],["dc.date.available","2022-03-01T11:45:54Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1038/nn.3183"],["dc.identifier.pii","BFnn3183"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103493"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1546-1726"],["dc.relation.issn","1097-6256"],["dc.rights.uri","http://www.springer.com/tdm"],["dc.title","Cooperation of Syd-1 with Neurexin synchronizes pre- with postsynaptic assembly"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","565"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","579"],["dc.bibliographiccitation.volume","188"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Schmidt, Manuela"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Christiansen, Frauke"],["dc.contributor.author","Zube, Christina"],["dc.contributor.author","Quentin, Christine"],["dc.contributor.author","Körner, Jorg"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2022-03-01T11:46:32Z"],["dc.date.available","2022-03-01T11:46:32Z"],["dc.date.issued","2010"],["dc.description.abstract","Active zones (AZs) are presynaptic membrane domains mediating synaptic vesicle fusion opposite postsynaptic densities (PSDs). At the Drosophila neuromuscular junction, the ELKS family member Bruchpilot (BRP) is essential for dense body formation and functional maturation of AZs. Using a proteomics approach, we identified Drosophila Syd-1 (DSyd-1) as a BRP binding partner. In vivo imaging shows that DSyd-1 arrives early at nascent AZs together with DLiprin-α, and both proteins localize to the AZ edge as the AZ matures. Mutants in dsyd-1 form smaller terminals with fewer release sites, and release less neurotransmitter. The remaining AZs are often large and misshapen, and ectopic, electron-dense accumulations of BRP form in boutons and axons. Furthermore, glutamate receptor content at PSDs increases because of excessive DGluRIIA accumulation. The AZ protein DSyd-1 is needed to properly localize DLiprin-α at AZs, and seems to control effective nucleation of newly forming AZs together with DLiprin-α. DSyd-1 also organizes trans-synaptic signaling to control maturation of PSD composition independently of DLiprin-α."],["dc.description.abstract","Active zones (AZs) are presynaptic membrane domains mediating synaptic vesicle fusion opposite postsynaptic densities (PSDs). At the Drosophila neuromuscular junction, the ELKS family member Bruchpilot (BRP) is essential for dense body formation and functional maturation of AZs. Using a proteomics approach, we identified Drosophila Syd-1 (DSyd-1) as a BRP binding partner. In vivo imaging shows that DSyd-1 arrives early at nascent AZs together with DLiprin-α, and both proteins localize to the AZ edge as the AZ matures. Mutants in dsyd-1 form smaller terminals with fewer release sites, and release less neurotransmitter. The remaining AZs are often large and misshapen, and ectopic, electron-dense accumulations of BRP form in boutons and axons. Furthermore, glutamate receptor content at PSDs increases because of excessive DGluRIIA accumulation. The AZ protein DSyd-1 is needed to properly localize DLiprin-α at AZs, and seems to control effective nucleation of newly forming AZs together with DLiprin-α. DSyd-1 also organizes trans-synaptic signaling to control maturation of PSD composition independently of DLiprin-α."],["dc.identifier.doi","10.1083/jcb.200908055"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103708"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","A Syd-1 homologue regulates pre- and postsynaptic maturation in Drosophila"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","667"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","683"],["dc.bibliographiccitation.volume","202"],["dc.contributor.author","Matkovic, Tanja"],["dc.contributor.author","Siebert, Matthias"],["dc.contributor.author","Knoche, Elena"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Schmidt, Manuela"],["dc.contributor.author","Thomas, Ulrich"],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Kamin, Dirk"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Buerger, Joerg"],["dc.contributor.author","Hollmann, Christina"],["dc.contributor.author","Mielke, Thorsten"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2017-09-07T11:47:38Z"],["dc.date.available","2017-09-07T11:47:38Z"],["dc.date.issued","2013"],["dc.description.abstract","Synaptic vesicles (SVs) fuse at a specialized membrane domain called the active zone (AZ), covered by a conserved cytomatrix. How exactly cytomatrix components intersect with SV release remains insufficiently understood. We showed previously that loss of the Drosophila melanogaster ELKS family protein Bruchpilot (BRP) eliminates the cytomatrix (T bar) and declusters Ca2+ channels. In this paper, we explored additional functions of the cytomatrix, starting with the biochemical identification of two BRP isoforms. Both isoforms alternated in a circular array and were important for proper T-bar formation. Basal transmission was decreased in isoform-specific mutants, which we attributed to a reduction in the size of the readily releasable pool (RRP) of SVs. We also found a corresponding reduction in the number of SVs docked close to the remaining cytomatrix. We propose that the macromolecular architecture created by the alternating pattern of the BRP isoforms determines the number of Ca2+ channel-coupled SV release slots available per AZ and thereby sets the size of the RRP."],["dc.identifier.doi","10.1083/jcb.201301072"],["dc.identifier.gro","3142305"],["dc.identifier.isi","000323319900007"],["dc.identifier.pmid","23960145"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6809"],["dc.language.iso","en"],["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","The Bruchpilot cytomatrix determines the size of the readily releasable pool of synaptic vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14340"],["dc.bibliographiccitation.issue","43"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","14345"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Hallermann, Stefan"],["dc.contributor.author","Kittel, Robert Johannes"],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Weyhersmueller, Annika"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Schwaerzel, Martin"],["dc.contributor.author","Sigrist, Stephan J."],["dc.contributor.author","Heckmann, Manfred"],["dc.date.accessioned","2018-11-07T08:37:54Z"],["dc.date.available","2018-11-07T08:37:54Z"],["dc.date.issued","2010"],["dc.description.abstract","At presynaptic active zones (AZs), the frequently observed tethering of synaptic vesicles to an electron-dense cytomatrix represents a process of largely unknown functional significance. Here, we identified a hypomorphic allele, brp(nude), lacking merely the last 1% of the C-terminal amino acids (17 of 1740) of the active zone protein Bruchpilot. In brp(nude), electron-dense bodies were properly shaped, though entirely bare of synaptic vesicles. While basal glutamate release was unchanged, paired-pulse and sustained stimulation provoked depression. Furthermore, rapid recovery following sustained release was slowed. Our results causally link, with intramolecular precision, the tethering of vesicles at the AZ cytomatrix to synaptic depression."],["dc.identifier.doi","10.1523/JNEUROSCI.2495-10.2010"],["dc.identifier.isi","000283790800008"],["dc.identifier.pmid","20980589"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18652"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Naked Dense Bodies Provoke Depression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9696"],["dc.bibliographiccitation.issue","26"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","9707"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Christiansen, Frauke"],["dc.contributor.author","Zube, Christina"],["dc.contributor.author","Andlauer, Till F. M."],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Fouquet, Wernher"],["dc.contributor.author","Owald, David"],["dc.contributor.author","Mertel, Sara"],["dc.contributor.author","Leiss, Florian"],["dc.contributor.author","Tavosanis, Gaia"],["dc.contributor.author","Luna, Abud J. Farca"],["dc.contributor.author","Fiala, Andre"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2018-11-07T08:54:56Z"],["dc.date.available","2018-11-07T08:54:56Z"],["dc.date.issued","2011"],["dc.description.abstract","Plastic changes at the presynaptic sites of the mushroom body (MB) principal neurons called Kenyon cells (KCs) are considered to represent a neuronal substrate underlying olfactory learning and memory. It is generally believed that presynaptic and postsynaptic sites of KCs are spatially segregated. In the MB calyx, KCs receive olfactory input from projection neurons (PNs) on their dendrites. Their presynaptic sites, however, are thought to be restricted to the axonal projections within the MB lobes. Here, we show that KCs also form presynapses along their calycal dendrites, by using novel transgenic tools for visualizing presynaptic active zones and postsynaptic densities. At these presynapses, vesicle release following stimulation could be observed. They reside at a distance from the PN input into the KC dendrites, suggesting that regions of presynaptic and postsynaptic differentiation are segregated along individual KC dendrites. KC presynapses are present in gamma-type KCs that support short-and long-term memory in adult flies and larvae. They can also be observed in alpha/beta-type KCs, which are involved in memory retrieval, but not in alpha'/beta'-type KCs, which are implicated in memory acquisition and consolidation. We hypothesize that, as in mammals, recurrent activity loops might operate for memory retrieval in the fly olfactory system. The newly identified KC-derived presynapses in the calyx are, inter alia, candidate sites for the formation of memory traces during olfactory learning."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 554, EXC 257]"],["dc.identifier.doi","10.1523/JNEUROSCI.6542-10.2011"],["dc.identifier.isi","000292189500028"],["dc.identifier.pmid","21715635"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22788"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Presynapses in Kenyon Cell Dendrites in the Mushroom Body Calyx of Drosophila"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]