Tuffy, Liam Patrick

[["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","321"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","446"],["dc.contributor.author","Poulopoulos, Alexandros"],["dc.contributor.author","Soykan, Tolga"],["dc.contributor.author","Tuffy, Liam P."],["dc.contributor.author","Hammer, Matthieu"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:48:25Z"],["dc.date.available","2017-09-07T11:48:25Z"],["dc.date.issued","2012"],["dc.description.abstract","Neuroligins are postsynaptic adhesion proteins involved in the establishment of functional synapses in the central nervous system. In rodents, four genes give rise to neuroligins that function at distinct synapses, with corresponding neurotransmitter and subtype specificities. In the present study, we examined the interactions between the different neuroligins by isolating endogenous oligomeric complexes using in situ cross-linking on primary neurons. Examining hippocampal, striatal, cerebellar and spinal cord cultures, we found that neuroligins form constitutive dimers, including homomers and, most notably, neuroligin 1/3 heteromers. Additionally, we found that neuroligin monomers are specifically retained in the secretory pathway through a cellular quality control mechanism that involves the neuroligin transmembrane domain, ensuring that dimerization occurs prior to cell surface trafficking. Lastly, we identified differences in the dimerization capacity of autism-associated neuroligin mutants, and found that neuroligin 3 R471C mutants can form heterodimers with neuroligin 1. The pervasive nature of neuroligin dimerization indicates that the unit of neuroligin function is the dimer, and raises intriguing possibilities of distinct heterodimer functions, and of interactions between native and mutant neuroligins contributing to disease phenotypes."],["dc.identifier.doi","10.1042/BJ20120808"],["dc.identifier.gro","3142468"],["dc.identifier.isi","000308767500016"],["dc.identifier.pmid","22671294"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8618"],["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","0264-6021"],["dc.title","Homodimerization and isoform-specific heterodimerization of neuroligins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","516"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","523"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Hammer, Matthieu"],["dc.contributor.author","Krueger-Burg, Dilja"],["dc.contributor.author","Tuffy, Liam Patrick"],["dc.contributor.author","Cooper, Benjamin Hillman"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Goswami, Sarit Pati"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.contributor.author","Jonas, Peter"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:46:34Z"],["dc.date.available","2017-09-07T11:46:34Z"],["dc.date.issued","2015"],["dc.description.abstract","Loss-of-function mutations in the synaptic adhesion protein Neuroligin-4 are among the most common genetic abnormalities associated with autism spectrum disorders, but little is known about the function of Neuroligin-4 and the consequences of its loss. We assessed synaptic and network characteristics in Neuroligin-4 knockout mice, focusing on the hippocampus as a model brain region with a critical role in cognition and memory, and found that Neuroligin-4 deletion causes subtle defects of the protein composition and function of GABAergic synapses in the hippocampal CA3 region. Interestingly, these subtle synaptic changes are accompanied by pronounced perturbations of γ-oscillatory network activity, which has been implicated in cognitive function and is altered in multiple psychiatric and neurodevelopmental disorders. Our data provide important insights into the mechanisms by which Neuroligin-4-dependent GABAergic synapses may contribute to autism phenotypes and indicate new strategies for therapeutic approaches."],["dc.identifier.doi","10.1016/j.celrep.2015.09.011"],["dc.identifier.gro","3150543"],["dc.identifier.pmid","26456829"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7316"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Perturbed Hippocampal Synaptic Inhibition and γ-Oscillations in a Neuroligin-4 Knockout Mouse Model of Autism"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]