Zeug, André

[["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Niebert, Markus"],["dc.contributor.author","Dityatev, Alexander"],["dc.contributor.author","Dityateva, Galina"],["dc.contributor.author","Gorinski, Nataliya"],["dc.contributor.author","Guseva, Daria"],["dc.contributor.author","Abdel-Galil, Dalia"],["dc.contributor.author","Fröhlich, Matthias"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2022-03-01T11:44:05Z"],["dc.date.available","2022-03-01T11:44:05Z"],["dc.date.issued","2012"],["dc.description.abstract","Serotonin receptors 5-HT1A and 5-HT7 are highly co-expressed in brain regions implicated in depression. However, their functional interaction has not been established. In the present study we show that 5-HT1A and 5-HT7 receptors form heterodimers both in vitro and in vivo. Foerster resonance energy transfer-based assays revealed that, in addition to heterodimers, homodimers composed either by 5-HT1A or 5-HT7 receptors together with monomers co-exist in cells. The highest affinity to form the complex was obtained for the 5-HT7-5-HT7 homodimers, followed by the 5-HT7-5-HT1A heterodimers and 5-HT1A-5-HT1A homodimers. Functionally, heterodimerization decreases 5-HT1A receptor-mediated activation of Gi-protein without affecting 5-HT7 receptor-mediated signalling. Moreover, heterodimerization markedly decreases the ability of the 5-HT1A receptor to activate G-protein gated inwardly rectifying potassium channels in a heterologous system. The inhibitory effect on such channels was also preserved in hippocampal neurons, demonstrating a physiological relevance of heteromerization in vivo. In addition, heterodimerization is critically involved in initiation of the serotonin-mediated 5-HT1A receptor internalization and also enhances the ability of the 5-HT1A receptor to activate the mitogen-activated protein kinases. Finally, we found that production of 5-HT7 receptors in hippocampus continuously decreases during postnatal development, indicating that the relative concentration of 5-HT1A-5-HT7 heterodimers and, consequently, their functional importance undergoes pronounced developmental changes."],["dc.description.abstract","Serotonin receptors 5-HT1A and 5-HT7 are highly co-expressed in brain regions implicated in depression. However, their functional interaction has not been established. In the present study we show that 5-HT1A and 5-HT7 receptors form heterodimers both in vitro and in vivo. Foerster resonance energy transfer-based assays revealed that, in addition to heterodimers, homodimers composed either by 5-HT1A or 5-HT7 receptors together with monomers co-exist in cells. The highest affinity to form the complex was obtained for the 5-HT7-5-HT7 homodimers, followed by the 5-HT7-5-HT1A heterodimers and 5-HT1A-5-HT1A homodimers. Functionally, heterodimerization decreases 5-HT1A receptor-mediated activation of Gi-protein without affecting 5-HT7 receptor-mediated signalling. Moreover, heterodimerization markedly decreases the ability of the 5-HT1A receptor to activate G-protein gated inwardly rectifying potassium channels in a heterologous system. The inhibitory effect on such channels was also preserved in hippocampal neurons, demonstrating a physiological relevance of heteromerization in vivo. In addition, heterodimerization is critically involved in initiation of the serotonin-mediated 5-HT1A receptor internalization and also enhances the ability of the 5-HT1A receptor to activate the mitogen-activated protein kinases. Finally, we found that production of 5-HT7 receptors in hippocampus continuously decreases during postnatal development, indicating that the relative concentration of 5-HT1A-5-HT7 heterodimers and, consequently, their functional importance undergoes pronounced developmental changes."],["dc.identifier.doi","10.1242/jcs.101337"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102922"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.title","Heterodimerization of serotonin receptors 5-HT1A and 5-HT7 differentially regulates receptor signalling and trafficking"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1821"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1827"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Zeug, André"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2022-03-01T11:44:56Z"],["dc.date.available","2022-03-01T11:44:56Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1016/j.bpj.2012.09.031"],["dc.identifier.pii","S0006349512010727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103164"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Quantitative Intensity-Based FRET Approaches—A Comparative Snapshot"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]