Holt, Matthew G.

[["dc.bibliographiccitation.firstpage","805"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U82"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Thutupalli, Shashi"],["dc.contributor.author","Risselada, J. H."],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Herminghaus, Stephan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:10Z"],["dc.date.available","2017-09-07T11:44:10Z"],["dc.date.issued","2011"],["dc.description.abstract","Synaptotagmin-1 triggers Ca2+-sensitive, rapid neurotransmitter release by promoting interactions between SNARE proteins on synaptic vesicles and the plasma membrane. How synaptotagmin-1 promotes this interaction is unclear, and the massive increase in membrane fusion efficiency of Ca2+-bound synaptotagmin-1 has not been reproduced in vitro. However, previous experiments have been performed at relatively high salt concentrations, screening potentially important electrostatic interactions. Using functional reconstitution in liposomes, we show here that at low ionic strength SNARE-mediated membrane fusion becomes strictly dependent on both Ca2+ and synaptotagmin-1. Under these conditions, synaptotagmin-1 functions as a distance regulator that tethers the liposomes too far from the plasma membrane for SNARE nucleation in the absence of Ca2+, but while bringing the liposomes close enough for membrane fusion in the presence of Ca2+. These results may explain how the relatively weak electrostatic interactions between synaptotagmin-1 and membranes substantially accelerate fusion."],["dc.identifier.doi","10.1038/nsmb.2061"],["dc.identifier.gro","3142704"],["dc.identifier.isi","000292507500009"],["dc.identifier.pmid","21642968"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/138"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9993"],["dc.title","Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","831"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","846"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Takamori, Shigeo"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Stenius, Katinka"],["dc.contributor.author","Lemke, Edward A."],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schenck, Stephan"],["dc.contributor.author","Brügger, Britta"],["dc.contributor.author","Ringler, Philippe"],["dc.contributor.author","Müller, Shirley A."],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Graeter, Frauke"],["dc.contributor.author","Hub, Jochen S."],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Mieskes, Gottfried"],["dc.contributor.author","Moriyama, Yoshinori"],["dc.contributor.author","Klingauf, Juergen"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Heuser, John"],["dc.contributor.author","Wieland, Felix"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:49:54Z"],["dc.date.available","2017-09-07T11:49:54Z"],["dc.date.issued","2006"],["dc.description.abstract","Membrane traffic in eukaryotic cells involves transport of vesicles that bud from a donor compartment and fuse with an acceptor compartment. Common principles of budding and fusion have emerged, and many of the proteins involved in these events are now known. However, a detailed picture of an entire trafficking organelle is not yet available. Using synaptic vesicles as a model, we have now determined the protein and lipid composition; measured vesicle size, density, and mass; calculated the average protein and lipid mass per vesicle; and determined the copy number of more than a dozen major constituents. A model has been constructed that integrates all quantitative data and includes structural models of abundant proteins. Synaptic vesicles are dominated by proteins, possess a surprising diversity of trafficking proteins, and, with the exception of the V-ATPase that is present in only one to two copies, contain numerous copies of proteins essential for membrane traffic and neurotransmitter uptake."],["dc.identifier.doi","10.1016/j.cell.2006.10.030"],["dc.identifier.gro","3143587"],["dc.identifier.isi","000242330600027"],["dc.identifier.pmid","17110340"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1117"],["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","0092-8674"],["dc.title","Molecular anatomy of a trafficking organelle"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1200"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1208"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Castorph, Simon"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Arleth, Lise"],["dc.contributor.author","Sztucki, Michael"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:46:06Z"],["dc.date.available","2017-09-07T11:46:06Z"],["dc.date.issued","2010"],["dc.description.abstract","Synaptic vesicles (SVs) are small, membrane-bound organelles that are found in the synaptic terminal of neurons, and which are crucial in neurotransmission. After a rise in internal [Ca2+] during neuronal stimulation, SVs fuse with the plasma membrane releasing their neurotransmitter content, which then signals neighboring neurons. SVs are subsequently recycled and refilled with neurotransmitter for further rounds of release. Recently, tremendous progress has been made in elucidating the molecular composition of SVs, as well as putative protein-protein interactions. However, what is lacking is an empirical description of SV structure at the supramolecular level which is necessary to enable us to fully understand the processes of membrane fusion, retrieval, and recycling. Using small-angle x-ray scattering, we have directly investigated the size and structure of purified SVs. From this information, we deduced detailed size and density parameters for the protein layers responsible for SV function, as well as information about the lipid bilayer. To achieve a convincing model fit, a laterally anisotropic structure for the protein shell is needed, as a rotationally symmetric density profile does not explain the data. Not only does our model confirm many of the preexisting ideas concerning SV structure, but also for the first time, to our knowledge, it indicates structural refinements, such as the presence of protein microdomains."],["dc.identifier.doi","10.1016/j.bpj.2009.12.4278"],["dc.identifier.gro","3142938"],["dc.identifier.isi","000276582700012"],["dc.identifier.pmid","20371319"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/397"],["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","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Structure Parameters of Synaptic Vesicles Quantified by Small-Angle X-Ray Scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","358"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U129"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Holt, Matthew G."],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Wouters, Fred S."],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2018-11-07T08:45:38Z"],["dc.date.available","2018-11-07T08:45:38Z"],["dc.date.issued","2010"],["dc.description.abstract","In eukaryotes, most intracellular membrane fusion reactions are mediated by the interaction of SNARE proteins that are present in both fusing membranes. However, the minimal number of SNARE complexes needed for membrane fusion is not known. Here we show unambiguously that one SNARE complex is sufficient for membrane fusion. We performed controlled in vitro Forster resonance energy transfer (FRET) experiments and found that liposomes bearing only a single SNARE molecule are still capable of fusion with other liposomes or with purified synaptic vesicles. Furthermore, we demonstrated that multiple SNARE complexes do not act cooperatively, showing that synergy between several SNARE complexes is not needed for membrane fusion. Our findings shed new light on the mechanism of SNARE-mediated membrane fusion and call for a revision of current views of fusion events such as the fast release of neurotransmitters."],["dc.identifier.doi","10.1038/nsmb.1748"],["dc.identifier.isi","000275182700017"],["dc.identifier.pmid","20139985"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20493"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1545-9993"],["dc.title","One SNARE complex is sufficient for membrane fusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","284a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Castorph, Simon"],["dc.contributor.author","Holt, Matthew G."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Arleth, Lise"],["dc.contributor.author","Sztucki, Michael"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2018-11-07T08:47:10Z"],["dc.date.available","2018-11-07T08:47:10Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1016/j.bpj.2009.12.1549"],["dc.identifier.isi","000208762002437"],["dc.identifier.pii","S0006349509033542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20881"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110209"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.issn","0006-3495"],["dc.title","Structure Analysis of Synaptic Vesicles by Solution Small-Angle Scattering of X-Rays"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1394"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1402"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Ghosh, Sajal Kumar"],["dc.contributor.author","Castorph, Simon"],["dc.contributor.author","Konovalov, Oleg"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Holt, Matthew"],["dc.date.accessioned","2017-09-07T11:48:56Z"],["dc.date.available","2017-09-07T11:48:56Z"],["dc.date.issued","2012"],["dc.description.abstract","Synaptic vesicles (SVs) are small, membrane-bound organelles that are found in the synaptic terminal of neurons. Although tremendous progress has been made in understanding the protein machinery that drives fusion of SVs with the presynaptic membrane, little progress has been made in understanding changes in the membrane structure that accompany this process. We used lipid monolayers of defined composition to mimic biological membranes, which were probed by x-ray reflectivity and grazing incidence x-ray diffraction. These techniques allowed us to successfully monitor structural changes in the membranes at molecular level, both in response to injection of SVs in the subphase below the monolayer, as well as to physiological cues involved in neurotransmitter release, such as increases in the concentration of the membrane lipid PIP2, or addition of physiological levels of Ca2+. Such structural changes may well modulate vesicle fusion in vivo."],["dc.identifier.doi","10.1016/j.bpj.2012.01.006"],["dc.identifier.gro","3142562"],["dc.identifier.isi","000301907400018"],["dc.identifier.pmid","22455922"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8926"],["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","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","membrane biophysics"],["dc.subject.gro","neuro biophysics"],["dc.title","Measuring Ca2+-Induced Structural Changes in Lipid Monolayers: Implications for Synaptic Vesicle Exocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","105"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Physiology"],["dc.bibliographiccitation.lastpage","130"],["dc.bibliographiccitation.volume","418"],["dc.contributor.author","Matthews, G."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Penner, R."],["dc.date.accessioned","2022-03-01T11:47:13Z"],["dc.date.available","2022-03-01T11:47:13Z"],["dc.date.issued","1989"],["dc.identifier.doi","10.1113/jphysiol.1989.sp017830"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103955"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0022-3751"],["dc.title","Second messenger-activated calcium influx in rat peritoneal mast cells."],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","8362"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Muhammad, Karzan"],["dc.contributor.author","Reddy-Alla, Suneel"],["dc.contributor.author","Driller, Jan H."],["dc.contributor.author","Schreiner, Dietmar"],["dc.contributor.author","Rey, Ulises"],["dc.contributor.author","Böhme, Mathias A."],["dc.contributor.author","Hollmann, Christina"],["dc.contributor.author","Ramesh, Niraja"],["dc.contributor.author","Depner, Harald"],["dc.contributor.author","Luetzkendorf, Janine"],["dc.contributor.author","Matkovic, Tanja"],["dc.contributor.author","Goetz, Torsten"],["dc.contributor.author","Bergeron, Dominique Dufour"],["dc.contributor.author","Schmoranzer, Jan"],["dc.contributor.author","Goettfert, Fabian"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Scheiffele, Peter"],["dc.contributor.author","Walter, Alexander Matthias"],["dc.contributor.author","Loll, Bernhard"],["dc.contributor.author","Sigrist, Stephan J."],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Assembly and maturation of synapses at the Drosophila neuromuscular junction (NMJ) depend on trans-synaptic neurexin/neuroligin signalling, which is promoted by the scaffolding protein Syd-1 binding to neurexin. Here we report that the scaffold protein spinophilin binds to the C-terminal portion of neurexin and is needed to limit neurexin/neuroligin signalling by acting antagonistic to Syd-1. Loss of presynaptic spinophilin results in the formation of excess, but atypically small active zones. Neuroligin-1/neurexin-1/Syd-1 levels are increased at spinophilin mutant NMJs, and removal of single copies of the neurexin-1, Syd-1 or neuroligin-1 genes suppresses the spinophilin-active zone phenotype. Evoked transmission is strongly reduced at spinophilin terminals, owing to a severely reduced release probability at individual active zones. We conclude that presynaptic spinophilin fine-tunes neurexin/neuroligin signalling to control active zone number and functionality, thereby optimizing them for action potential-induced exocytosis."],["dc.identifier.doi","10.1038/ncomms9362"],["dc.identifier.gro","3141812"],["dc.identifier.isi","000364921600002"],["dc.identifier.pmid","26471740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1346"],["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","2041-1723"],["dc.title","Presynaptic spinophilin tunes neurexin signalling to control active zone architecture and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","131"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Physiology"],["dc.bibliographiccitation.lastpage","144"],["dc.bibliographiccitation.volume","418"],["dc.contributor.author","Matthews, G."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Penner, R."],["dc.date.accessioned","2022-03-01T11:47:13Z"],["dc.date.available","2022-03-01T11:47:13Z"],["dc.date.issued","1989"],["dc.identifier.doi","10.1113/jphysiol.1989.sp017831"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103956"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0022-3751"],["dc.title","Chloride conductance activated by external agonists and internal messengers in rat peritoneal mast cells."],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]