Papadopoulos, Theofilos

[["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.contributor.author","George, Shanu"],["dc.contributor.author","Bear, John"],["dc.contributor.author","Taylor, Michael J."],["dc.contributor.author","Kanamalla, Karthik"],["dc.contributor.author","Fekete, Christopher D."],["dc.contributor.author","Chiou, Tzu‐Ting"],["dc.contributor.author","Miralles, Celia P."],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","De Blas, Angel L."],["dc.date.accessioned","2021-04-14T08:30:03Z"],["dc.date.available","2021-04-14T08:30:03Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1111/jnc.15270"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83084"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.title","Collybistin SH3‐protein isoforms are expressed in the rat brain promoting gephyrin and GABA‐A receptor clustering at GABAergic synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","8256"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","8270"],["dc.bibliographiccitation.volume","290"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Schemm, Rudolf"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2018-03-08T09:21:22Z"],["dc.date.available","2018-03-08T09:21:22Z"],["dc.date.issued","2015"],["dc.description.abstract","Signaling at nerve cell synapses is a key determinant of proper brain function, and synaptic defects—or synaptopathies—are at the basis of many neurological and psychiatric disorders. In key areas of the mammalian brain, such as the hippocampus or the basolateral amygdala, the clustering of the scaffolding protein Gephyrin and of γ-aminobutyric acid type A receptors at inhibitory neuronal synapses is critically dependent upon the brain-specific guanine nucleotide exchange factor Collybistin (Cb). Accordingly, it was discovered recently that an R290H missense mutation in the diffuse B-cell lymphoma homology domain of Cb, which carries the guanine nucleotide exchange factor activity, leads to epilepsy and intellectual disability in human patients. In the present study, we determined the mechanism by which the CbR290H mutation perturbs inhibitory synapse formation and causes brain dysfunction. Based on a combination of biochemical, cell biological, and molecular dynamics simulation approaches, we demonstrate that the R290H mutation alters the strength of intramolecular interactions between the diffuse B-cell lymphoma homology domain and the pleckstrin homology domain of Cb. This defect reduces the phosphatidylinositol 3-phosphate binding affinity of Cb, which limits its normal synaptogenic activity. Our data indicate that impairment of the membrane lipid binding activity of Cb and a consequent defect in inhibitory synapse maturation represent a likely molecular pathomechanism of epilepsy and mental retardation in humans."],["dc.identifier.doi","10.1074/jbc.M114.633024"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12859"],["dc.language.iso","en"],["dc.notes.intern","GRO-Li-Import"],["dc.notes.status","final"],["dc.relation.doi","10.1074/jbc.M114.633024"],["dc.relation.issn","0021-9258"],["dc.relation.issn","1083-351X"],["dc.title","Lipid Binding Defects and Perturbed Synaptogenic Activity of a Collybistin R290H Mutant That Causes Epilepsy and Intellectual Disability"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","100709"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.volume","296"],["dc.contributor.author","Wagner, Sven"],["dc.contributor.author","Lee, ChoongKu"],["dc.contributor.author","Rojas, Lucia"],["dc.contributor.author","Specht, Christian G."],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.date.accessioned","2021-06-01T10:49:40Z"],["dc.date.available","2021-06-01T10:49:40Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.jbc.2021.100709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86372"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","0021-9258"],["dc.title","The α3 subunit of GABAA receptors promotes formation of inhibitory synapses in the absence of collybistin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2113"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","2133"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Schneeberger, Daniela"],["dc.contributor.author","Tria, Giancarlo"],["dc.contributor.author","Buechner, Claudia"],["dc.contributor.author","Bader, Nicole"],["dc.contributor.author","Svergun, Dmitri"],["dc.contributor.author","Tessmer, Ingrid"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.contributor.author","Schindelin, Hermann"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:45:30Z"],["dc.date.available","2017-09-07T11:45:30Z"],["dc.date.issued","2014"],["dc.description.abstract","The formation of neuronal synapses and the dynamic regulation of their efficacy depend on the assembly of the postsynaptic neuro transmitter receptor apparatus. Receptor recruitment to inhibitory GABAergic and glycinergic synapses is controlled by the scaffold protein gephyrin and the adaptor protein collybistin. We derived new insights into the structure of collybistin and used these to design biochemical, cell biological, and genetic analyses of collybistin function. Our data define a collybistin-based protein interaction network that controls the gephyrin content of inhibitory postsynapses. Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides. This function of collybistin is regulated by binding of the adhesion protein neuroligin-2, which stabilizes the open/active conformation of collybistin at the postsynaptic plasma membrane by competing with an intramolecular interaction in collybistin that favors the closed/inactive conformation. By linking trans-synaptic neuroligin-dependent adhesion and phosphoinositide signaling with gephyrin recruitment, the collybistin-based regulatory switch mechanism represents an integrating regulatory node in the formation and function of inhibitory postsynapses."],["dc.identifier.doi","10.15252/embj.201488143"],["dc.identifier.gro","3142051"],["dc.identifier.isi","000342503000012"],["dc.identifier.pmid","25082542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4000"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","A conformational switch in collybistin determines the differentiation of inhibitory postsynapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","412"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Current Opinion in Neurobiology"],["dc.bibliographiccitation.lastpage","422"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Krueger, Dilja D."],["dc.contributor.author","Tuffy, Liam P."],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","Neurexins (NXs) and neuroligins (NLs) are transsynaptically interacting cell adhesion proteins that play a key role in the formation, maturation, activity-dependent validation, and maintenance of synapses. As complex alternative splicing processes in nerve cells generate a large number of NX and NLs variants, it has been proposed that a combinatorial interaction code generated by these variants may determine synapse identity and network connectivity during brain development. The functional importance of NXs and NLs is exemplified by the fact that mutations in NX and NL genes are associated with several neuropsychiatric disorders, most notably with autism. Accordingly, major research efforts have focused on the molecular mechanisms by which NXs and NLs operate at synapses. In this review, we summarize recent progress in this field and discuss emerging topics, such as the role of alternative interaction partners of NXs and NLs in synapse formation and function, and their relevance for synaptic plasticity in the mature brain. The novel findings highlight the fundamental importance of NX-NL interactions in a wide range of synaptic functions."],["dc.identifier.doi","10.1016/j.conb.2012.02.012"],["dc.identifier.gro","3142522"],["dc.identifier.isi","000306634700008"],["dc.identifier.pmid","22424845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8882"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Current Biology Ltd"],["dc.relation.issn","0959-4388"],["dc.title","The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10119"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","10130"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Um, Ji Won"],["dc.contributor.author","Choii, Gayoung"],["dc.contributor.author","Park, Dongseok"],["dc.contributor.author","Kim, Dongwook"],["dc.contributor.author","Jeon, Sangmin"],["dc.contributor.author","Kang, Hyeyeon"],["dc.contributor.author","Mori, Takuma"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Yoo, Taesun"],["dc.contributor.author","Lee, Yeunkum"],["dc.contributor.author","Kim, Eunjoon"],["dc.contributor.author","Tabuchi, Katsuhiko"],["dc.contributor.author","Ko, Jaewon"],["dc.date.accessioned","2020-12-10T18:12:55Z"],["dc.date.available","2020-12-10T18:12:55Z"],["dc.date.issued","2016"],["dc.description.abstract","Gephyrin is a central scaffold protein that mediates development, function, and plasticity of mammalian inhibitory synapses by interacting with various inhibitory synaptic proteins. Here, we show that IQSLC3, a guanine nucleotide exchange factor for ARE6, directly interacts with gephyrin, an interaction that is critical for the inhibitory synapse localization of IQSEC3. Overexpression of IQSEC3 increases inhibitory, but not excitatory, synapse density in a guanine nucleotide exchange factor activity-dependent manner. Conversely, knockdown of IQSEC3 decreases size of gephyrin cluster without altering gephyrin puncta density. Collectively, these data reveal that IQSEC3 acts together with gephyrin to regulate inhibitory synapse development."],["dc.identifier.doi","10.1074/jbc.M115.712893"],["dc.identifier.eissn","1083-351X"],["dc.identifier.isi","000375602800023"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","27002143"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74535"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","IQ Motif and SEC7 Domain-containing Protein 3 (IQSEC3) Interacts with Gephyrin to Promote Inhibitory Synapse Formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs232835"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Mayer, Simone"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Roehse, Heiko"],["dc.contributor.author","Hentrich, Jennifer"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.date.accessioned","2020-12-10T18:41:54Z"],["dc.date.available","2020-12-10T18:41:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/jcs.232835"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77720"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A GTPase-induced switch in phospholipid affinity of collybistin contributes to synaptic gephyrin clustering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","66"],["dc.bibliographiccitation.journal","Current Opinion in Neurobiology"],["dc.bibliographiccitation.lastpage","77"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Krueger-Burg, Dilja"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2018-03-08T09:21:31Z"],["dc.date.available","2018-03-08T09:21:31Z"],["dc.date.issued","2017"],["dc.description.abstract","While the postsynaptic density of excitatory synapses is known to encompass a highly complex molecular machinery, the equivalent organizational structure of inhibitory synapses has long remained largely undefined. In recent years, however, substantial progress has been made towards identifying the full complement of organizational proteins present at inhibitory synapses, including submembranous scaffolds, intracellular signaling proteins, transsynaptic adhesion proteins, and secreted factors. Here, we summarize these findings and discuss future challenges in assigning synapse-specific functions to the newly discovered catalog of proteins, an endeavor that will depend heavily on newly developed technologies such as proximity biotinylation. Further advances are made all the more essential by growing evidence that links inhibitory synapses to psychiatric and neurological disorders."],["dc.identifier.doi","10.1016/j.conb.2017.04.003"],["dc.identifier.pmid","28460365"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12904"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/10"],["dc.language.iso","en"],["dc.notes.intern","GRO-Li-Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P10: Rekrutierung und Verankerung von Neurotransmitterrezeptoren an GABAergen Synapsen - Zellbiologie und molekulare Mechanismen"],["dc.relation.doi","10.1016/j.conb.2017.04.003"],["dc.relation.issn","0959-4388"],["dc.relation.issn","0959-4388"],["dc.relation.workinggroup","RG Brose"],["dc.title","Organizers of inhibitory synapses come of age"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","overview_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20795"],["dc.bibliographiccitation.issue","51"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","20800"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Mayer, Simone"],["dc.contributor.author","Kumar, Rohit"],["dc.contributor.author","Jaiswal, Mamta"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Ahmadian, Mohammad Reza"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Betz, Heinrich"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.date.accessioned","2017-09-07T11:46:59Z"],["dc.date.available","2017-09-07T11:46:59Z"],["dc.date.issued","2013"],["dc.description.abstract","In many brain regions, gephyrin and GABA(A) receptor clustering at developing inhibitory synapses depends on the guanine nucleotide exchange factor collybistin (Cb). The vast majority of Cb splice variants contain an autoinhibitory src homology 3 domain, and several synaptic proteins are known to bind to this SH3 domain and to thereby activate gephyrin clustering. However, many functional GABAergic synapses form independently of the known Cb-activating proteins, indicating that additional Cb activators must exist. Here we show that the small Rho-like GTPase TC10 stimulates Cb-dependent gephyrin clustering by binding in its active, GTP-bound state to the pleckstrin homology domain of Cb. Overexpression of a constitutively active TC10 variant in neurons causes an increase in the density of synaptic gephyrin clusters and mean miniature inhibitory postsynaptic current amplitudes, whereas a dominant negative TC10 variant has opposite effects. The enhancement of Cb-induced gephyrin clustering by GTP-TC10 does not depend on the guanine nucleotide exchange activity of Cb but involves an interaction that resembles reported interactions of other small GTPases with their effectors. Our data indicate that GTP-TC10 activates the major src homology 3 domain-containing Cb variants by relieving autoinhibition and thus define an alternative GTPase-driven signaling pathway in the genesis of inhibitory synapses."],["dc.identifier.doi","10.1073/pnas.1309078110"],["dc.identifier.gro","3142233"],["dc.identifier.isi","000328548600093"],["dc.identifier.pmid","24297911"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6010"],["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","Collybistin activation by GTP-TC10 enhances postsynaptic gephyrin clustering and hippocampal GABAergic neurotransmission"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]