Zhang, Weiqi

[["dc.bibliographiccitation.firstpage","741"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","754"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Rawson, Randi L."],["dc.contributor.author","Mohrmann, Ralf"],["dc.contributor.author","Missler, Markus"],["dc.contributor.author","Gottmann, Kurt"],["dc.contributor.author","Zhang, Weiqi"],["dc.contributor.author","Suedhof, Thomas C."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:52:32Z"],["dc.date.available","2017-09-07T11:52:32Z"],["dc.date.issued","2006"],["dc.description.abstract","Synaptogenesis, the generation and maturation of functional synapses between nerve cells, is an essential step in the development of neuronal networks in the brain. It is thought to be triggered by members of the neuroligin family of postsynaptic cell adhesion proteins, which may form transsynaptic contacts with presynaptic alpha- and beta-neurexins and have been implicated in the etiology of autism. We show that deletion mutant mice lacking neuroligin expression die shortly after birth due to respiratory failure. This respiratory failure is a consequence of reduced GABAergic/glycinergic and glutamatergic synaptic transmission and network activity in brainstem centers that control respiration. However, the density of synaptic contacts is not altered in neuroligin-deficient brains and cultured neurons. Our data show that neuroligins are required for proper synapse maturation and brain function, but not for the initial formation of synaptic contacts."],["dc.identifier.doi","10.1016/j.neuron.2006.09.003"],["dc.identifier.gro","3143623"],["dc.identifier.isi","000240997900013"],["dc.identifier.pmid","16982420"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1158"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIMH NIH HHS [MH52804-08]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0896-6273"],["dc.title","Neuroligins determine synapse maturation 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","628"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","642"],["dc.bibliographiccitation.volume","63"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Meyer, Guido"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Hoon, Mrinalini"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Zhang, Mingyue"],["dc.contributor.author","Paarmann, Ingo"],["dc.contributor.author","Fuchs, Celine"],["dc.contributor.author","Harvey, Kirsten"],["dc.contributor.author","Jedlicka, Peter"],["dc.contributor.author","Schwarzacher, Stephan W."],["dc.contributor.author","Betz, Heinrich"],["dc.contributor.author","Harvey, Robert J."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Zhang, Weiqi"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.date.accessioned","2017-09-07T11:46:51Z"],["dc.date.available","2017-09-07T11:46:51Z"],["dc.date.issued","2009"],["dc.description.abstract","In the mammalian CNS, each neuron typically receives thousands of synaptic inputs from diverse classes of neurons. Synaptic transmission to the postsynaptic neuron relies on localized and transmitter-specific differentiation of the plasma membrane with postsynaptic receptor, scaffolding, and adhesion proteins accumulating in precise apposition to presynaptic sites of transmitter release. We identified protein interactions of the synaptic adhesion molecule neuroligin 2 that drive postsynaptic differentiation at inhibitory synapses. Neuroligin 2 binds the scaffolding protein gephyrin through a conserved cytoplasmic motif and functions as a specific activator of collybistin, thus guiding membrane tethering of the inhibitory postsynaptic scaffold. Complexes of neuroligin 2, gephyrin and collybistin are sufficient for cell-autonomous clustering of inhibitory neurotransmitter receptors. Deletion of neuroligin 2 in mice perturbs GABAergic and glycinergic synaptic transmission and leads to a loss of postsynaptic specializations specifically at perisomatic inhibitory synapses."],["dc.identifier.doi","10.1016/j.neuron.2009.08.023"],["dc.identifier.gro","3143057"],["dc.identifier.isi","000269852300010"],["dc.identifier.pmid","19755106"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/529"],["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","Neuroligin 2 Drives Postsynaptic Assembly at Perisomatic Inhibitory Synapses through Gephyrin and Collybistin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4330"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","4342"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Zhang, W."],["dc.contributor.author","Rohlmann, A."],["dc.contributor.author","Sargsyan, Vardanush"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Hammer, Robert E."],["dc.contributor.author","Sudhof, T. C."],["dc.contributor.author","Missler, Markus"],["dc.date.accessioned","2018-11-07T11:07:39Z"],["dc.date.available","2018-11-07T11:07:39Z"],["dc.date.issued","2005"],["dc.description.abstract","Neurexins constitute a large family of highly variable cell-surface molecules that may function in synaptic transmission and/or synapse formation. Each of the three known neurexin genes encodes two major neurexin variants, alpha- and beta-neurexins, that are composed of distinct extracellular domains linked to identical intracellular sequences. Deletions of one, two, or all three alpha-neurexins in mice recently demonstrated their essential role at synapses. In multiple alpha-neurexin knock-outs, neurotransmitter release from excitatory and inhibitory synapses was severely reduced, primarily probably because voltage-dependent Ca2+ channels were impaired. It remained unclear, however, which neurexin variants actually influence exocytosis and Ca2+ channels, which domain of neurexins is required for this function, and which Ca2+-channel subtypes are regulated. Here, we show by electrophysiological recordings that transgenic neurexin 1 alpha rescues the release and Ca2+-current phenotypes, whereas transgenic neurexin 1 beta has no effect, indicating the importance of the extracellular sequences for the function of neurexins. Because neurexin 1 alpha rescued the knock-out phenotype independent of the alpha-neurexin gene deleted, these data are consistent with a redundant function among different alpha-neurexins. In both knock-out and transgenically rescued mice, alpha-neurexins selectively affected the component of neurotransmitter release that depended on activation of N- and P/Q-type Ca2+ channels, but left L-type Ca2+ channels unscathed. Our findings indicate that alpha-neurexins represent organizer molecules in neurotransmission that regulate N- and P/Q-type Ca2+ channels, constituting an essential role at synapses that critically involves the extracellular domains of neurexins."],["dc.identifier.doi","10.1523/JNEUROSCI.0497-05.2005"],["dc.identifier.isi","000228702900014"],["dc.identifier.pmid","15858059"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52615"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Extracellular domains of alpha-neurexins participate in regulating synaptic transmission by selectively affecting N- and P/Q-type Ca2+ channels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8797"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","8806"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Matzke, Alexandra"],["dc.contributor.author","Sargsyan, Vardanush"],["dc.contributor.author","Holtmann, Bettina"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Asan, Esther"],["dc.contributor.author","Sendtner, Michael"],["dc.contributor.author","Pace, Giuseppina"],["dc.contributor.author","Howells, Norma"],["dc.contributor.author","Zhang, W."],["dc.contributor.author","Ponta, Helmut"],["dc.contributor.author","Orian-Rousseau, Veronique"],["dc.date.accessioned","2018-11-07T10:49:37Z"],["dc.date.available","2018-11-07T10:49:37Z"],["dc.date.issued","2007"],["dc.description.abstract","Recent evidence has shown that the activation of receptor tyrosine kinases is not only dependent on binding of their ligands but in addition requires adhesion molecules as coreceptors. We have identified CD44v6 as a coreceptor for c-Met in several tumor and primary cells. The CD44v6 ectodomain is required for c-Met activation, whereas the cytoplasmic tail recruits ERM proteins and the cytoskeleton into a signalosome complex. Here we demonstrate that c-Met (and hepatocyte growth factor and Gab1) is haploinsufficient in a cd44(-/-) background, as the cd44(-/-); met(-/-) (and cd44(-/-); hgf(+/-) and cd44(-/-); gab1(+/-)) mice die at birth. They have impaired synaptic transmission in the respiratory rhythm-generating network and alterations in the phrenic nerve. These results are the first genetic data showing that CD44 and c-Met collaborate in vivo and that they are involved in synaptogenesis and axon myelination in the central and peripheral nervous systems."],["dc.identifier.doi","10.1128/MCB.01355-07"],["dc.identifier.isi","000251527300032"],["dc.identifier.pmid","17923692"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48468"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Haploinsufficiency of c-met in cd44(-/-) mice identifies a collaboration of CD44 and c-met in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","International Journal of Developmental Neuroscience"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Sieber, M."],["dc.contributor.author","Storm, R."],["dc.contributor.author","Martinez-de-la-Torre, M."],["dc.contributor.author","Mueller, T."],["dc.contributor.author","Vasyutina, E."],["dc.contributor.author","Dutschmann, Mathias"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Zhang, W."],["dc.contributor.author","Birchmeier, Carmen"],["dc.date.accessioned","2018-11-07T08:54:08Z"],["dc.date.available","2018-11-07T08:54:08Z"],["dc.date.issued","2006"],["dc.format.extent","590"],["dc.identifier.doi","10.1016/j.ijdevneu.2006.09.279"],["dc.identifier.isi","000243663700276"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22602"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.conference","16th Biennial Meeting of the International-Society-for-Developmental-Neuroscience"],["dc.relation.eventlocation","Banff, CANADA"],["dc.relation.issn","0736-5748"],["dc.title","The homeodomain factor Lbx1 controls the differentiation of sensory relay neurons in the hindbrain"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","112"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Neurophysiology"],["dc.bibliographiccitation.lastpage","121"],["dc.bibliographiccitation.volume","99"],["dc.contributor.author","Medrihan, Lucian"],["dc.contributor.author","Tantalaki, Evangelia"],["dc.contributor.author","Aramuni, Gayane"],["dc.contributor.author","Sargsyan, Vardanush"],["dc.contributor.author","Dudanova, Irina"],["dc.contributor.author","Missler, Markus"],["dc.contributor.author","Zhang, W."],["dc.date.accessioned","2018-11-07T11:20:15Z"],["dc.date.available","2018-11-07T11:20:15Z"],["dc.date.issued","2008"],["dc.description.abstract","Rett syndrome is a neurodevelopmental disorder caused by mutations in the transcriptional repressor methyl-CpG- binding protein 2 (MeCP2) and represents the leading genetic cause for mental retardation in girls. MeCP2-mutant mice have been generated to study the molecular mechanisms of the disease. It was suggested that an imbalance between excitatory and inhibitory neurotransmission is responsible for the behavioral abnormalities, although it remained largely unclear which synaptic components are affected and how cellular impairments relate to the time course of the disease. Here, we report that MeCP2 KO mice present an imbalance between inhibitory and excitatory synaptic transmission in the ventrolateral medulla already at postnatal day 7. Focusing on the inhibitory synaptic transmission we show that GABAergic, but not glycinergic, synaptic transmission is strongly depressed in MeCP2 KO mice. These alterations are presumably due to both decreased presynaptic gamma-aminobutyric acid (GABA) release with reduced levels of the vesicular inhibitory transmitter transporter and reduced levels of postsynaptic GABA(A)-receptor subunits alpha 2 and alpha 4. Our data indicate that in the MeCP2 -/y mice specific synaptic molecules and signaling pathways are impaired in the brain stem during early postnatal development. These observations mandate the search for more refined diagnostic tools and may provide a rationale for the timing of future therapeutic interventions in Rett patients."],["dc.identifier.doi","10.1152/jn.00826.2007"],["dc.identifier.isi","000252398500010"],["dc.identifier.pmid","18032561"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55490"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","0022-3077"],["dc.title","Early defects of GABAergic synapses in the brain stem of a MeCP2 mouse model of Rett syndrome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]