Schmidt, Manuela

[["dc.bibliographiccitation.firstpage","3640"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3651"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Swan, Laura E."],["dc.contributor.author","Schmidt, Manuela"],["dc.contributor.author","Schwarz, Tobias"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.contributor.author","Prange, Ulrike"],["dc.contributor.author","Boeckers, Tobias"],["dc.contributor.author","Thomas, Ulrich"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2018-11-07T09:26:09Z"],["dc.date.available","2018-11-07T09:26:09Z"],["dc.date.issued","2006"],["dc.description.abstract","Glutamate receptor interacting protein (GRIP) homologues, initially characterized in synaptic glutamate receptor trafficking, consist of seven PDZ domains (PDZDs), whose conserved arrangement is of unknown significance. The Drosophila GRIP homologue (DGrip) is needed for proper guidance of embryonic somatic muscles towards epidermal attachment sites, with both excessive and reduced DGrip activity producing specific phenotypes in separate muscle groups. These phenotypes were utilized to analyze the molecular architecture underlying DGrip signaling function in vivo. Surprisingly, removing PDZDs 1-3 (DGrip Delta 1-3) or deleting ligand binding in PDZDs 1 or 2 convert DGrip to excessive in vivo activity mediated by ligand binding to PDZD 7. Yeast two-hybrid screening identifies the cell adhesion protein Echinoid's (Ed) type II PDZD-interaction motif as binding PDZDs 1, 2 and 7 of DGrip. ed loss-of-function alleles exhibit muscle defects, enhance defects caused by reduced DGrip activity and suppress the dominant DGrip Delta 1-3 effect during embryonic muscle formation. We propose that Ed and DGrip form a signaling complex, where competition between N-terminal and the C-terminal PDZDs of DGrip for Ed binding controls signaling function."],["dc.identifier.doi","10.1038/sj.emboj.7601216"],["dc.identifier.isi","000239626000020"],["dc.identifier.pmid","16858411"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30235"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Complex interaction of Drosophila GRIP PDZ domains and Echinoid during muscle morphogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1051"],["dc.bibliographiccitation.issue","5776"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1054"],["dc.bibliographiccitation.volume","312"],["dc.contributor.author","Kittel, Robert J."],["dc.contributor.author","Wichmann, Carolin"],["dc.contributor.author","Rasse, T. M."],["dc.contributor.author","Fouquet, W."],["dc.contributor.author","Schmidt, Manuela"],["dc.contributor.author","Schmid, Andreas"],["dc.contributor.author","Wagh, D. A."],["dc.contributor.author","Pawlu, C."],["dc.contributor.author","Kellner, Robert R."],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Buchner, E."],["dc.contributor.author","Heckmann, M."],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2017-09-07T11:52:42Z"],["dc.date.available","2017-09-07T11:52:42Z"],["dc.date.issued","2006"],["dc.description.abstract","The molecular organization of presynaptic active zones during calcium influx - triggered neurotransmitter release is the focus of intense investigation. The Drosophila coiled-coil domain protein Bruchpilot (BRP) was observed in donut-shaped structures centered at active zones of neuromuscular synapses by using subdiffraction resolution STED ( stimulated emission depletion) fluorescence microscopy. At brp mutant active zones, electron-dense projections (T-bars) were entirely lost, Ca2+ channels were reduced in density, evoked vesicle release was depressed, and short-term plasticity was altered. BRP-like proteins seem to establish proximity between Ca2+ channels and vesicles to allow efficient transmitter release and patterned synaptic plasticity."],["dc.identifier.doi","10.1126/science.1126308"],["dc.identifier.gro","3143688"],["dc.identifier.isi","000237628800045"],["dc.identifier.pmid","16614170"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1229"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0036-8075"],["dc.title","Bruchpilot promotes active zone assembly, Ca2+ channel clustering, and vesicle release"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["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"]]