Rhee, Jeong-Seop

[["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","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","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.journal","Molecular Psychiatry"],["dc.contributor.author","Ambrozkiewicz, Mateusz C."],["dc.contributor.author","Borisova, Ekaterina"],["dc.contributor.author","Schwark, Manuela"],["dc.contributor.author","Ripamonti, Silvia"],["dc.contributor.author","Schaub, Theres"],["dc.contributor.author","Smorodchenko, Alina"],["dc.contributor.author","Weber, A. Ioana"],["dc.contributor.author","Rhee, Hong Jun"],["dc.contributor.author","Altas, Bekir"],["dc.contributor.author","Yilmaz, Rüstem"],["dc.contributor.author","Mueller, Susanne"],["dc.contributor.author","Piepkorn, Lars"],["dc.contributor.author","Horan, Stephen T."],["dc.contributor.author","Straussberg, Rachel"],["dc.contributor.author","Zaqout, Sami"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Dere, Ekrem"],["dc.contributor.author","Rosário, Marta"],["dc.contributor.author","Boehm-Sturm, Philipp"],["dc.contributor.author","Borck, Guntram"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Tarabykin, Victor"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.date.accessioned","2020-12-10T18:09:37Z"],["dc.date.available","2020-12-10T18:09:37Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41380-020-0714-8"],["dc.identifier.eissn","1476-5578"],["dc.identifier.issn","1359-4184"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73708"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The murine ortholog of Kaufman oculocerebrofacial syndrome protein Ube3b regulates synapse number by ubiquitinating Ppp3cc"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13205"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13210"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Hsia, Hung-En"],["dc.contributor.author","Kumar, Rohit"],["dc.contributor.author","Luca, Rossella"],["dc.contributor.author","Takeda, Michiko"],["dc.contributor.author","Courchet, Julien"],["dc.contributor.author","Nakashima, Jonathan"],["dc.contributor.author","Wu, Shumin"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","An, Wenlin"],["dc.contributor.author","Eickholt, Britta J."],["dc.contributor.author","Polleux, Franck"],["dc.contributor.author","Rotin, Daniela"],["dc.contributor.author","Wu, Hong"],["dc.contributor.author","Rossner, Moritz J."],["dc.contributor.author","Bagni, Claudia"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.date.accessioned","2017-09-07T11:45:33Z"],["dc.date.available","2017-09-07T11:45:33Z"],["dc.date.issued","2014"],["dc.description.abstract","Protein ubiquitination is a core regulatory determinant of neural development. Previous studies have indicated that the Nedd4-family E3 ubiquitin ligases Nedd4-1 and Nedd4-2 may ubiquitinate phosphatase and tensin homolog (PTEN) and thereby regulate axonal growth in neurons. Using conditional knockout mice, we show here that Nedd4-1 and Nedd4-2 are indeed required for axonal growth in murine central nervous system neurons. However, in contrast to previously published data, we demonstrate that PTEN is not a substrate of Nedd4-1 and Nedd4-2, and that aberrant PTEN ubiquitination is not involved in the impaired axon growth upon deletion of Nedd4-1 and Nedd4-2. Rather, PTEN limits Nedd4-1 protein levels by modulating the activity of mTORC1, a protein complex that controls protein synthesis and cell growth. Our data demonstrate that Nedd4-family E3 ligases promote axonal growth and branching in the developing mammalian brain, where PTEN is not a relevant substrate. Instead, PTEN controls neurite growth by regulating Nedd4-1 expression."],["dc.identifier.doi","10.1073/pnas.1400737111"],["dc.identifier.gro","3142055"],["dc.identifier.isi","000341625600056"],["dc.identifier.pmid","25157163"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4045"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Ubiquitin E3 ligase Nedd4-1 acts as a downstream target of PI3K/PTEN-mTORC1 signaling to promote neurite growth"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1143"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","1161"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Kaeser, Pascal S."],["dc.contributor.author","Hirrlinger, Johannes"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Nestvogel, Dennis"],["dc.contributor.author","Kalla, Stefan"],["dc.contributor.author","Fejtova, Anna"],["dc.contributor.author","Verrier, Sophie E."],["dc.contributor.author","Bungers, Simon R."],["dc.contributor.author","Cooper, Benjamin H."],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Wang, Yun"],["dc.contributor.author","Nehring, Ralf B."],["dc.contributor.author","Gundelfinger, Eckart D."],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Südhof, Thomas C."],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2018-01-09T16:08:02Z"],["dc.date.available","2018-01-09T16:08:02Z"],["dc.date.issued","2017"],["dc.description.abstract","Presynaptic active zones (AZs) are unique subcellular structures at neuronal synapses, which contain a network of specific proteins that control synaptic vesicle (SV) tethering, priming, and fusion. Munc13s are core AZ proteins with an essential function in SV priming. In hippocampal neurons, two different Munc13s-Munc13-1 and bMunc13-2-mediate opposite forms of presynaptic short-term plasticity and thus differentially affect neuronal network characteristics. We found that most presynapses of cortical and hippocampal neurons contain only Munc13-1, whereas ∼10% contain both Munc13-1 and bMunc13-2. Whereas the presynaptic recruitment and activation of Munc13-1 depends on Rab3-interacting proteins (RIMs), we demonstrate here that bMunc13-2 is recruited to synapses by the AZ protein ELKS1, but not ELKS2, and that this recruitment determines basal SV priming and short-term plasticity. Thus, synapse-specific interactions of different Munc13 isoforms with ELKS1 or RIMs are key determinants of the molecular and functional heterogeneity of presynaptic AZs."],["dc.identifier.doi","10.1083/jcb.201606086"],["dc.identifier.pmid","28264913"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11622"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1540-8140"],["dc.relation.haserratum","/handle/2/11623"],["dc.title","ELKS1 localizes the synaptic vesicle priming protein bMunc13-2 to a specific subset of active zones"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","358"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","372"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Neeb, Antje"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Young, Samuel M., Jr."],["dc.contributor.author","Takeda, Michiko"],["dc.contributor.author","Katsurabayashi, Shutaro"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Malakhova, Oxana A."],["dc.contributor.author","Zhang, Dong-Er"],["dc.contributor.author","Ulmilkawa, Masato"],["dc.contributor.author","Kariya, Ken-ichi"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Nedd4-1 is a \"neuronal precursor cell expressed and developmentally downregulated protein\" and among the most abundant E3 ubiquitin ligases in mammalian neurons. In analyses of conventional and conditional Nedd4-1-deficient mice, we found that Nedd4-1 plays a critical role in dendrite formation. Nedd4-1, the serine/threonine kinase TNIK, and Rap2A form a complex that controls Nedd4-1-mediated ubiquitination of Rap2A. Ubiquitination by Nedd4-1 inhibits Rap2A function, which reduces the activity of Rap2 effector kinases of the TNIK family and promotes dendrite growth. We conclude that a Nedd4-1/Rap2A/TNIK signaling pathway regulates neurite growth and arborization in mammalian neurons."],["dc.identifier.doi","10.1016/j.neuron.2010.01.007"],["dc.identifier.gro","3142966"],["dc.identifier.isi","000275185200009"],["dc.identifier.pmid","20159449"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/428"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0896-6273"],["dc.title","Regulation of Rap2A by the Ubiquitin Ligase Nedd4-1 Controls Neurite Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]