Cooper, Benjamin Hillman

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Tawfik, Bassam"],["dc.contributor.author","Martins, Joana S."],["dc.contributor.author","Houy, Sébastien"],["dc.contributor.author","Imig, Cordelia"],["dc.contributor.author","Pinheiro, Paulo S."],["dc.contributor.author","Wojcik, Sonja M."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Sørensen, Jakob Balslev"],["dc.date.accessioned","2022-03-01T11:44:34Z"],["dc.date.available","2022-03-01T11:44:34Z"],["dc.date.issued","2021"],["dc.description.abstract","Synaptotagmins confer calcium-dependence to the exocytosis of secretory vesicles, but how coexpressed synaptotagmins interact remains unclear. We find that synaptotagmin-1 and synaptotagmin-7 when present alone act as standalone fast and slow Ca 2+ -sensors for vesicle fusion in mouse chromaffin cells. When present together, synaptotagmin-1 and synaptotagmin-7 are found in largely non-overlapping clusters on dense-core vesicles. Synaptotagmin-7 stimulates Ca 2+ -dependent vesicle priming and inhibits depriming, and it promotes ubMunc13-2- and phorbolester-dependent priming, especially at low resting calcium concentrations. The priming effect of synaptotagmin-7 increases the number of vesicles fusing via synaptotagmin-1, while negatively affecting their fusion speed, indicating both synergistic and competitive interactions between synaptotagmins. Synaptotagmin-7 places vesicles in close membrane apposition (<6 nm); without it, vesicles accumulate out of reach of the fusion complex (20–40 nm). We suggest that a synaptotagmin-7-dependent movement toward the membrane is involved in Munc13-2/phorbolester/Ca 2+ -dependent priming as a prelude to fast and slow exocytosis triggering."],["dc.description.abstract","Synaptotagmins confer calcium-dependence to the exocytosis of secretory vesicles, but how coexpressed synaptotagmins interact remains unclear. We find that synaptotagmin-1 and synaptotagmin-7 when present alone act as standalone fast and slow Ca 2+ -sensors for vesicle fusion in mouse chromaffin cells. When present together, synaptotagmin-1 and synaptotagmin-7 are found in largely non-overlapping clusters on dense-core vesicles. Synaptotagmin-7 stimulates Ca 2+ -dependent vesicle priming and inhibits depriming, and it promotes ubMunc13-2- and phorbolester-dependent priming, especially at low resting calcium concentrations. The priming effect of synaptotagmin-7 increases the number of vesicles fusing via synaptotagmin-1, while negatively affecting their fusion speed, indicating both synergistic and competitive interactions between synaptotagmins. Synaptotagmin-7 places vesicles in close membrane apposition (<6 nm); without it, vesicles accumulate out of reach of the fusion complex (20–40 nm). We suggest that a synaptotagmin-7-dependent movement toward the membrane is involved in Munc13-2/phorbolester/Ca 2+ -dependent priming as a prelude to fast and slow exocytosis triggering."],["dc.identifier.doi","10.7554/eLife.64527"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103054"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2050-084X"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Synaptotagmin-7 places dense-core vesicles at the cell membrane to promote Munc13-2- and Ca2+-dependent priming"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","882"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.volume","84"],["dc.contributor.author","Imig, Cordelia"],["dc.contributor.author","Min, Sang-Won"],["dc.contributor.author","Krinner, Stefanie"],["dc.contributor.author","Arancillo, Marife"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Südhof, Thomas C."],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Cooper, Benjamin H."],["dc.date.accessioned","2022-03-01T11:45:21Z"],["dc.date.available","2022-03-01T11:45:21Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.neuron.2014.11.003"],["dc.identifier.pii","S0896627314010034"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103296"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0896-6273"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","The Morphological and Molecular Nature of Synaptic Vesicle Priming at Presynaptic Active Zones"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","1197"],["dc.contributor.author","Cooper, Ben"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Flügge, Gabriele"],["dc.date.accessioned","2022-10-06T13:33:00Z"],["dc.date.available","2022-10-06T13:33:00Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1016/j.brainres.2007.11.066"],["dc.identifier.pii","S0006899307028429"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115519"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","0006-8993"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Glycoprotein M6a is present in glutamatergic axons in adult rat forebrain and cerebellum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8040"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","The Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","8052"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Cooper, Benjamin"],["dc.contributor.author","Hemmerlein, Maike"],["dc.contributor.author","Ammermüller, Josef"],["dc.contributor.author","Imig, Cordelia"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Kalla, Stefan"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Brandstätter, Johann Helmut"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","Munc13 proteins are essential regulators of exocytosis. In hippocampal glutamatergic neurons, the genetic deletion of Munc13s results in the complete loss of primed synaptic vesicles (SVs) in direct contact with the presynaptic active zone membrane, and in a total block of neurotransmitter release. Similarly drastic consequences of Munc13 loss are detectable in hippocampal and striatal GABAergic neurons. We show here that, in the adult mouse retina, the two Munc13-2 splice variants bMunc13-2 and ubMunc13-2 are selectively localized to conventional and ribbon synapses, respectively, and that ubMunc13-2 is the only Munc13 isoform in mature photoreceptor ribbon synapses. Strikingly, the genetic deletion of ubMunc13-2 has little effect on synaptic signaling by photoreceptor ribbon synapses and does not prevent membrane attachment of synaptic vesicles at the photoreceptor ribbon synaptic site. Thus, photoreceptor ribbon synapses and conventional synapses differ fundamentally with regard to their dependence on SV priming proteins of the Munc13 family. Their function is only moderately affected by Munc13 loss, which leads to slight perturbations of signal integration in the retina."],["dc.identifier.doi","10.1523/JNEUROSCI.4240-11.2012"],["dc.identifier.gro","3142521"],["dc.identifier.isi","000305091800028"],["dc.identifier.pmid","22674279"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8881"],["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","0270-6474"],["dc.title","Munc13-Independent Vesicle Priming at Mouse Photoreceptor Ribbon Synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e3659"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Cooper, Ben"],["dc.contributor.author","Fuchs, Eberhard"],["dc.contributor.author","Fluegge, Gabriele"],["dc.date.accessioned","2018-11-07T08:33:25Z"],["dc.date.available","2018-11-07T08:33:25Z"],["dc.date.issued","2009"],["dc.description.abstract","It has been repeatedly shown that chronic stress changes dendrites, spines and modulates expression of synaptic molecules. These effects all may impair information transfer between neurons. The present study shows that chronic stress also regulates expression of M6a, a glycoprotein which is localised in axonal membranes. We have previously demonstrated that M6a is a component of glutamatergic axons. The present data reveal that it is the splice variant M6a-Ib, not M6a-Ia, which is strongly expressed in the brain. Chronic stress in male rats (3 weeks daily restraint) has regional effects: quantitative in situ hybridization demonstrated that M6a-Ib mRNA in dentate gyrus granule neurons and in CA3 pyramidal neurons is downregulated, whereas M6a-Ib mRNA in the medial prefrontal cortex is upregulated by chronic stress. This is the first study showing that expression of an axonal membrane molecule is differentially affected by stress in a region-dependent manner. Therefore, one may speculate that diminished expression of the glycoprotein in the hippocampus leads to altered output in the corresponding cortical projection areas. Enhanced M6a-Ib expression in the medial prefrontal cortex (in areas prelimbic and infralimbic cortex) might be interpreted as a compensatory mechanism in response to changes in axonal projections from the hippocampus. Our findings provide evidence that in addition to alterations in dendrites and spines chronic stress also changes the integrity of axons and may thus impair information transfer even between distant brain regions."],["dc.identifier.doi","10.1371/journal.pone.0003659"],["dc.identifier.isi","000265483100001"],["dc.identifier.pmid","19180239"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5822"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17571"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Expression of the Axonal Membrane Glycoprotein M6a Is Regulated by Chronic Stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3632"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","3643.e8"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Maus, Lydia"],["dc.contributor.author","Lee, ChoongKu"],["dc.contributor.author","Altas, Bekir"],["dc.contributor.author","Sertel, Sinem M."],["dc.contributor.author","Weyand, Kirsten"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Imig, Cordelia"],["dc.contributor.author","Cooper, Benjamin H."],["dc.date.accessioned","2020-12-10T14:23:02Z"],["dc.date.available","2020-12-10T14:23:02Z"],["dc.date.issued","2020"],["dc.description.abstract","Although similar in molecular composition, synapses can exhibit strikingly distinct functional transmitter release and plasticity characteristics. To determine whether ultrastructural differences co-define this functional heterogeneity, we combine hippocampal organotypic slice cultures, high-pressure freezing, freeze substitution, and 3D-electron tomography to compare two functionally distinct synapses: hippocampal Schaffer collateral and mossy fiber synapses. We find that mossy fiber synapses, which exhibit a lower release probability and stronger short-term facilitation than Schaffer collateral synapses, harbor lower numbers of docked synaptic vesicles at active zones and a second pool of possibly tethered vesicles in their vicinity. Our data indicate that differences in the ratio of docked versus tethered vesicles at active zones contribute to distinct functional characteristics of synapses."],["dc.identifier.doi","10.1016/j.celrep.2020.02.083"],["dc.identifier.pmid","32187536"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71813"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/51"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/36"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A01: Die Ultrastruktur der Synapse in Aktion"],["dc.relation.workinggroup","RG Brose"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Cooper"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Ultrastructural Correlates of Presynaptic Functional Heterogeneity in Hippocampal Synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","304"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","311.e4"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Sigler, Albrecht"],["dc.contributor.author","Oh, Won Chan"],["dc.contributor.author","Imig, Cordelia"],["dc.contributor.author","Altas, Bekir"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Kwon, Hyung-Bae"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2018-03-08T09:21:30Z"],["dc.date.available","2018-03-08T09:21:30Z"],["dc.date.issued","2017"],["dc.description.abstract","Dendritic spines are the major transmitter reception compartments of glutamatergic synapses in most principal neurons of the mammalian brain and play a key role in the function of nerve cell circuits. The formation of functional spine synapses is thought to be critically dependent on presynaptic glutamatergic signaling. By analyzing CA1 pyramidal neurons in mutant hippocampal slice cultures that are essentially devoid of presynaptic transmitter release, we demonstrate that the formation and maintenance of dendrites and functional spines are independent of synaptic glutamate release."],["dc.identifier.doi","10.1016/j.neuron.2017.03.029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12901"],["dc.language.iso","en"],["dc.notes.intern","GRO-Li-Import"],["dc.notes.status","final"],["dc.relation.doi","10.1016/j.neuron.2017.03.029"],["dc.relation.issn","0896-6273"],["dc.title","Formation and Maintenance of Functional Spines in the Absence of Presynaptic Glutamate Release"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14687"],["dc.bibliographiccitation.issue","44"],["dc.bibliographiccitation.journal","The Journal of neuroscience"],["dc.bibliographiccitation.lastpage","14696"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Ishiyama, Shimpei"],["dc.contributor.author","Schmidt, Hartmut"],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Eilers, Jens"],["dc.date.accessioned","2017-09-07T11:45:26Z"],["dc.date.available","2017-09-07T11:45:26Z"],["dc.date.issued","2014"],["dc.description.abstract","Munc13-3 is a presynaptic protein implicated in vesicle priming that is strongly expressed in cerebellar granule cells (GCs). Mice deficient of Munc13-3 (Munc13-3(-/-)) show an increased paired-pulse ratio (PPR), which led to the hypothesis that Munc13-3 increases the release probability (p(r)) of vesicles. In the present study, we analyzed unitary synaptic connections between GCs and basket cells in acute cerebellar slices from wild-type and Munc13-3(-/-) mice. Unitary EPSCs recorded from Munc13-3(-/-) GCs showed normal kinetics and synaptic latency but a significantly increased PPR and fraction of synaptic failures. A quantal analysis revealed that neither the charge of single quanta nor the binominal parameter N were affected by loss of Munc13-3 but that pr was almost halved in Munc13-3(-/-). Neither presynaptic Ca2+ influx was affected by deletion of Munc13-3 nor replenishment of the readily releasable vesicle pool. However, a high concentration of EGTA led to a reduction in EPSCs that was significantly stronger in Munc13-3(-/-). We conclude that Munc13-3 is responsible for an additional step of molecular and/or positional \"superpriming\" that substantially increases the efficacy of Ca2+-triggered release."],["dc.identifier.doi","10.1523/JNEUROSCI.2060-14.2014"],["dc.identifier.gro","3142030"],["dc.identifier.isi","000345220100018"],["dc.identifier.pmid","25355221"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3767"],["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","0270-6474"],["dc.title","Munc13-3 Superprimes Synaptic Vesicles at Granule Cell-to-Basket Cell Synapses in the Mouse Cerebellum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Daniel, James A."],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Palvimo, Jorma J."],["dc.contributor.author","Zhang, Fu-Ping"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Tirard, Marilyn"],["dc.date.accessioned","2022-03-01T11:44:23Z"],["dc.date.available","2022-03-01T11:44:23Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.3389/fncel.2018.00117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103011"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1662-5102"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Response: Commentary: Analysis of SUMO1-conjugation at synapses"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","82"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","96"],["dc.bibliographiccitation.volume","79"],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Sakaba, Takeshi"],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Lin, Kun-Han"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Ashery, Uri"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Short-term synaptic plasticity, the dynamic alteration of synaptic strength during high-frequency activity, is a fundamental characteristic of all synapses. At the calyx of Held, repetitive activity eventually results in short-term synaptic depression, which is in part due to the gradual exhaustion of releasable synaptic vesicles. This is counterbalanced by Ca²⁺-dependent vesicle replenishment, but the molecular mechanisms of this replenishment are largely unknown. We studied calyces of Held in knockin mice that express a Ca²⁺-Calmodulin insensitive Munc13-1(W464R) variant of the synaptic vesicle priming protein Munc13-1. Calyces of these mice exhibit a slower rate of synaptic vesicle replenishment, aberrant short-term depression and reduced recovery from synaptic depression after high-frequency stimulation. Our data establish Munc13-1 as a major presynaptic target of Ca²⁺-Calmodulin signaling and show that the Ca²⁺-Calmodulin-Munc13-1 complex is a pivotal component of the molecular machinery that determines short-term synaptic plasticity characteristics."],["dc.identifier.doi","10.1016/j.neuron.2013.05.011"],["dc.identifier.gro","3142326"],["dc.identifier.isi","000321802000011"],["dc.identifier.pmid","23770256"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7042"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0896-6273"],["dc.title","Dynamic Control of Synaptic Vesicle Replenishment and Short-Term Plasticity by Ca²⁺-Calmodulin-Munc13-1 Signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]