Brose, Nils

[["dc.bibliographiccitation.firstpage","16522"],["dc.bibliographiccitation.issue","26"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","16523"],["dc.bibliographiccitation.volume","99"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Neher, Erwin"],["dc.date.accessioned","2017-09-07T11:45:11Z"],["dc.date.available","2017-09-07T11:45:11Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1073/pnas.022708199"],["dc.identifier.gro","3144145"],["dc.identifier.isi","000180101600006"],["dc.identifier.pmid","12486246"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1737"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Specificity emerges in the dissection of diacylglycerol- and protein kinase C-mediated signalling pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1243"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Biology and Evolution"],["dc.bibliographiccitation.lastpage","1258"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Maxeiner, Stephan"],["dc.contributor.author","Benseler, Fritz"],["dc.contributor.author","Krasteva-Christ, Gabriela"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Südhof, Thomas C"],["dc.contributor.editor","Nowick, Katja"],["dc.date.accessioned","2022-03-01T11:46:46Z"],["dc.date.available","2022-03-01T11:46:46Z"],["dc.date.issued","2020"],["dc.description.abstract","Abstract Variants in genes encoding synaptic adhesion proteins of the neuroligin family, most notably neuroligin-4, are a significant cause of autism spectrum disorders in humans. Although human neuroligin-4 is encoded by two genes, NLGN4X and NLGN4Y, that are localized on the X-specific and male-specific regions of the two sex chromosomes, the chromosomal localization and full genomic sequence of the mouse Nlgn4 gene remain elusive. Here, we analyzed the neuroligin-4 genes of numerous rodent species by direct sequencing and bioinformatics, generated complete drafts of multiple rodent neuroligin-4 genes, and examined their evolution. Surprisingly, we find that the murine Nlgn4 gene is localized to the pseudoautosomal region (PAR) of the sex chromosomes, different from its human orthologs. We show that the sequence differences between various neuroligin-4 proteins are restricted to hotspots in which rodent neuroligin-4 proteins contain short repetitive sequence insertions compared with neuroligin-4 proteins from other species, whereas all other protein sequences are highly conserved. Evolutionarily, these sequence insertions initiate in the clade eumuroidea of the infraorder myomorpha and are additionally associated with dramatic changes in noncoding sequences and gene size. Importantly, these changes are not exclusively restricted to neuroligin-4 genes but reflect major evolutionary changes that substantially altered or even deleted genes from the PARs of both sex chromosomes. Our results show that despite the fact that the PAR in rodents and the neuroligin-4 genes within the rodent PAR underwent massive evolutionary changes, neuroligin-4 proteins maintained a highly conserved core structure, consistent with a substantial evolutionary pressure preserving its physiological function."],["dc.description.abstract","Abstract Variants in genes encoding synaptic adhesion proteins of the neuroligin family, most notably neuroligin-4, are a significant cause of autism spectrum disorders in humans. Although human neuroligin-4 is encoded by two genes, NLGN4X and NLGN4Y, that are localized on the X-specific and male-specific regions of the two sex chromosomes, the chromosomal localization and full genomic sequence of the mouse Nlgn4 gene remain elusive. Here, we analyzed the neuroligin-4 genes of numerous rodent species by direct sequencing and bioinformatics, generated complete drafts of multiple rodent neuroligin-4 genes, and examined their evolution. Surprisingly, we find that the murine Nlgn4 gene is localized to the pseudoautosomal region (PAR) of the sex chromosomes, different from its human orthologs. We show that the sequence differences between various neuroligin-4 proteins are restricted to hotspots in which rodent neuroligin-4 proteins contain short repetitive sequence insertions compared with neuroligin-4 proteins from other species, whereas all other protein sequences are highly conserved. Evolutionarily, these sequence insertions initiate in the clade eumuroidea of the infraorder myomorpha and are additionally associated with dramatic changes in noncoding sequences and gene size. Importantly, these changes are not exclusively restricted to neuroligin-4 genes but reflect major evolutionary changes that substantially altered or even deleted genes from the PARs of both sex chromosomes. Our results show that despite the fact that the PAR in rodents and the neuroligin-4 genes within the rodent PAR underwent massive evolutionary changes, neuroligin-4 proteins maintained a highly conserved core structure, consistent with a substantial evolutionary pressure preserving its physiological function."],["dc.identifier.doi","10.1093/molbev/msaa014"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103791"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1537-1719"],["dc.relation.issn","0737-4038"],["dc.title","Evolution of the Autism-Associated Neuroligin-4 Gene Reveals Broad Erosion of Pseudoautosomal Regions in Rodents"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2477"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","2478"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:45:57Z"],["dc.date.available","2017-09-07T11:45:57Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.4161/cc.9.13.12236"],["dc.identifier.gro","3142893"],["dc.identifier.isi","000281205400004"],["dc.identifier.pmid","20543564"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/348"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1538-4101"],["dc.title","The ubiquitin E3 ligase Nedd4-1 controls neurite development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","102"],["dc.bibliographiccitation.journal","Current Opinion in Neurobiology"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Schreiner, Dietmar"],["dc.contributor.author","Savas, Jeffrey N."],["dc.contributor.author","Herzog, Etienne"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","de Wit, Joris"],["dc.date.accessioned","2017-09-07T11:52:19Z"],["dc.date.available","2017-09-07T11:52:19Z"],["dc.date.issued","2017"],["dc.description.abstract","The neural connectome is a critical determinant of brain function. Circuits of precisely wired neurons, and the features of transmission at the synapses connecting them, are thought to dictate information processing in the brain. While recent technological advances now allow to define the anatomical and functional neural connectome at unprecedented resolution, the elucidation of the molecular mechanisms that establish the precise patterns of connectivity and the functional characteristics of synapses has remained challenging. Here, we describe the power and limitations of genetic approaches in the analysis of mechanisms that control synaptic connectivity and function, and discuss how recent methodological developments in proteomics might be used to elucidate the molecular synaptic connectome that is at the basis of the neural connectome."],["dc.identifier.doi","10.1016/j.conb.2016.12.004"],["dc.identifier.gro","3144893"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2568"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0959-4388"],["dc.title","Synapse biology in the ‘circuit-age’—paths toward molecular connectomics"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","411"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Nature Neuroscience"],["dc.bibliographiccitation.lastpage","413"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Nouvian, Régis"],["dc.contributor.author","Neef, Jakob"],["dc.contributor.author","Bulankina, Anna V"],["dc.contributor.author","Reisinger, Ellen"],["dc.contributor.author","Pangršič, Tina"],["dc.contributor.author","Frank, Thomas"],["dc.contributor.author","Sikorra, Stefan"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Binz, Thomas"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2017-09-07T11:44:19Z"],["dc.date.available","2017-09-07T11:44:19Z"],["dc.date.issued","2011"],["dc.description.abstract","SNARE proteins mediate membrane fusion. Neurosecretion depends on neuronal soluble NSF attachment protein receptors ( SNAREs; SNAP-25, syntaxin-1, and synaptobrevin-1 or synaptobrevin-2) and is blocked by neurotoxin-mediated cleavage or genetic ablation. We found that exocytosis in mouse inner hair cells (IHCs) was insensitive to neurotoxins and genetic ablation of neuronal SNAREs. mRNA, but no synaptically localized protein, of neuronal SNAREs was present in IHCs. Thus, IHC exocytosis is unconventional and may operate independently of neuronal SNAREs."],["dc.identifier.doi","10.1038/nn.2774"],["dc.identifier.gro","3142757"],["dc.identifier.isi","000288849400007"],["dc.identifier.pmid","21378973"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/196"],["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","1097-6256"],["dc.title","Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Ripamonti, Silvia"],["dc.contributor.author","Ambrozkiewicz, Mateusz C."],["dc.contributor.author","Guzzi, Francesca"],["dc.contributor.author","Gravati, Marta"],["dc.contributor.author","Biella, Gerardo"],["dc.contributor.author","Bormuth, Ingo"],["dc.contributor.author","Hammer, Matthieu"],["dc.contributor.author","Tuffy, Liam P."],["dc.contributor.author","Sigler, Albrecht"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Nishimori, Katsuhiko"],["dc.contributor.author","Toselli, Mauro"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Parenti, Marco"],["dc.contributor.author","Rhee, JeongSeop"],["dc.date.accessioned","2018-03-08T09:21:30Z"],["dc.date.available","2018-03-08T09:21:30Z"],["dc.date.issued","2017"],["dc.description.abstract","Beyond its role in parturition and lactation, oxytocin influences higher brain processes that control social behavior of mammals, and perturbed oxytocin signaling has been linked to the pathogenesis of several psychiatric disorders. However, it is still largely unknown how oxytocin exactly regulates neuronal function. We show that early, transient oxytocin exposure in vitro inhibits the development of hippocampal glutamatergic neurons, leading to reduced dendrite complexity, synapse density, and excitatory transmission, while sparing GABAergic neurons. Conversely, genetic elimination of oxytocin receptors increases the expression of protein components of excitatory synapses and excitatory synaptic transmission in vitro. In vivo, oxytocin-receptor-deficient hippocampal pyramidal neurons develop more complex dendrites, which leads to increased spine number and reduced γ-oscillations. These results indicate that oxytocin controls the development of hippocampal excitatory neurons and contributes to the maintenance of a physiological excitation/inhibition balance, whose disruption can cause neurobehavioral disturbances."],["dc.identifier.doi","10.7554/eLife.22466"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12900"],["dc.language.iso","en"],["dc.notes.intern","GRO-Li-Import"],["dc.notes.status","final"],["dc.relation.doi","10.7554/eLife.22466"],["dc.relation.eissn","2050-084X"],["dc.title","Transient oxytocin signaling primes the development and function of excitatory hippocampal neurons"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","22663"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","22671"],["dc.bibliographiccitation.volume","268"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Gasic, G. P."],["dc.contributor.author","Vetter, D. E."],["dc.contributor.author","Sullivan, John M."],["dc.contributor.author","Heinemann, S. F."],["dc.date.accessioned","2017-09-07T11:51:32Z"],["dc.date.available","2017-09-07T11:51:32Z"],["dc.date.issued","1993"],["dc.description.abstract","In the rat central nervous system, the mRNA encoding the N-methyl-D-aspartate receptor subunit R1 is the most ubiquitously distributed among the cloned subunit mRNAs of this glutamate receptor subtype. The N-methyl-D-aspartate R1 mRNA is very abundantly expressed and N-methyl-D-aspartate R1 coexpression is necessary for functional expression of all other cloned N-methyl-D-aspartate receptor subunits. Therefore, the R1 subunit is likely to be an essential component of all known N-methyl-D-aspartate receptors in rat brain. By employing sequence specific polyclonal antibodies, we demonstrate that rat brain N-methyl-D-aspartate R1, as well as recombinantly expressed receptor protein, has an apparent molecular mass of 116 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The receptor protein is heavily glycosylated. It is specifically localized to the central nervous system, and it coenriches with synaptic membranes upon subcellular fractionation of the cerebral cortex. Chemical cross-linking of synaptic membrane proteins shows that the N-methyl-D-aspartate R1 protein is part of a receptor protein complex with a molecular mass of 730 kDa. By using immunocytochemical methods, we demonstrate a widespread but distinct distribution of N-methyl-D-aspartate R1 in neurons of the rat brain, with prominent immunostaining in certain layers of the cerebral cortex, in the hippocampus and dentate gyrus, as well as in the cerebellum."],["dc.identifier.gro","3144763"],["dc.identifier.isi","A1993MD34800071"],["dc.identifier.pmid","8226775"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2423"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NINDS NIH HHS [NS 28706, NS 11549]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","123"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","136"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Betz, Andrea"],["dc.contributor.author","Ashery, Uri"],["dc.contributor.author","Rickmann, Michael"],["dc.contributor.author","Augustin, Iris"],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Südhof, Thomas C."],["dc.contributor.author","Rettig, Jens"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:48:09Z"],["dc.date.available","2017-09-07T11:48:09Z"],["dc.date.issued","1998"],["dc.description.abstract","Munc13-1, a mammalian homolog of C. elegans unc-13p, is thought to be involved in the regulation of synaptic transmission. We now demonstrate that Munc13-1 is a presynaptic high-affinity phorbol ester and diacylglycerol receptor with ligand affinities similar to those of protein kinase C. Munc13-1 associates with the plasma membrane in response to phorbol ester binding and acts as a phorbol ester-dependent enhancer of transmitter release when overexpressed presynaptically in the Xenopus neuromuscular junction. These observations establish Munc13-1 as a novel presynaptic target of the diacylglycerol second messenger pathway that acts in parallel with protein kinase C to regulate neurotransmitter secretion."],["dc.identifier.doi","10.1016/S0896-6273(00)80520-6"],["dc.identifier.gro","3144539"],["dc.identifier.isi","000075061900012"],["dc.identifier.pmid","9697857"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2174"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.eissn","1097-4199"],["dc.relation.issn","0896-6273"],["dc.title","Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S39"],["dc.bibliographiccitation.journal","Neuroscience Research"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Katsurabayashi, Shutaro"],["dc.contributor.author","Neeb, Antje"],["dc.contributor.author","Umikawa, Masato"],["dc.contributor.author","Kariya, Ken-ichi"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2022-03-01T11:45:18Z"],["dc.date.available","2022-03-01T11:45:18Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1016/j.neures.2007.06.228"],["dc.identifier.pii","S016801020700421X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103283"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0168-0102"],["dc.title","Regulation of dendritic development by E3 ubiquitin ligase Nedd4"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1067"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","1077"],["dc.bibliographiccitation.volume","190"],["dc.contributor.author","Liu, Yuanyuan"],["dc.contributor.author","Schirra, Claudia"],["dc.contributor.author","Edelmann, Ludwig"],["dc.contributor.author","Matti, Ulf"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Hof, Detlef"],["dc.contributor.author","Bruns, Dieter"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Rieger, Heiko"],["dc.contributor.author","Stevens, David R."],["dc.contributor.author","Rettig, Jens"],["dc.date.accessioned","2017-09-07T11:45:19Z"],["dc.date.available","2017-09-07T11:45:19Z"],["dc.date.issued","2010"],["dc.description.abstract","Priming of large dense-core vesicles (LDCVs) is a Ca(2+)-dependent step by which LDCVs enter a release-ready pool, involving the formation of the soluble N-ethyl-maleimide sensitive fusion protein attachment protein (SNAP) receptor complex consisting of syntaxin, SNAP-25, and synaptobrevin. Using mice lacking both isoforms of the calcium-dependent activator protein for secretion (CAPS), we show that LDCV priming in adrenal chromaffin cells entails two distinct steps. CAPS is required for priming of the readily releasable LDCV pool and sustained secretion in the continued presence of high Ca(2+) concentrations. Either CAPS1 or CAPS2 can rescue secretion in cells lacking both CAPS isoforms. Furthermore, the deficit in the readily releasable LDCV pool resulting from CAPS deletion is reversed by a constitutively open form of syntaxin but not by Munc13-1, a priming protein that facilitates the conversion of syntaxin to the open conformation. Our data indicate that CAPS functions downstream of Munc13s but also interacts functionally with Munc13s in the LDCV-priming process."],["dc.identifier.doi","10.1083/jcb.201001164"],["dc.identifier.gro","3142860"],["dc.identifier.isi","000282604600012"],["dc.identifier.pmid","20855507"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/310"],["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","Two distinct secretory vesicle-priming steps in adrenal chromaffin cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]