Lang, Thorsten

[["dc.bibliographiccitation.firstpage","2701"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","2706"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Brandhorst, Dorothea"],["dc.contributor.author","Zwilling, Daniel"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lippert, Undine"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:53:17Z"],["dc.date.available","2017-09-07T11:53:17Z"],["dc.date.issued","2006"],["dc.description.abstract","Membrane fusion in the secretory pathway is mediated by soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins. Different fusion steps are thought to be effected by independent sets of SNAREs, but it is unclear whether specificity is determined by an intrinsic specificity of SNARE pairing or by upstream factors. Using a newly developed microscopy-based assay, we have investigated the SNARE specificity of homotypic early endosomal fusion.. We show that early endosomes contain multiple sets of SNAREs, including, in addition to the putative early endosomal SNAREs, those involved in exocytosis and in fusion of late endosomes. We demonstrate that fusion is largely mediated by a complex formed by syntaxin 13, syntaxin 6, vti1a, and VAMP4, whereas the exocytic and late endosomal SNAREs play little or no role in the reaction. In contrast, proteoliposomes reconstituted with early endosomal SNAREs promiscuously fuse with liposomes containing exocytotic or late endosomal SNAREs. We conclude that the specificity of SNARE pairing does not suffice to determine the specificity of organelle fusion."],["dc.identifier.doi","10.1073/pnas.0511138103"],["dc.identifier.gro","3143735"],["dc.identifier.isi","000235554900041"],["dc.identifier.pmid","16469845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1282"],["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","0027-8424"],["dc.title","Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","502"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Pharmacology"],["dc.bibliographiccitation.lastpage","513"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Glebov, Konstantin"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Papusheva, Ekaterina"],["dc.contributor.author","Balakrishnan, Saju"],["dc.contributor.author","Keller, Bernhard U."],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2018-11-07T10:59:14Z"],["dc.date.available","2018-11-07T10:59:14Z"],["dc.date.issued","2007"],["dc.description.abstract","In the present study, we have used wild- type and palmitoylationdeficient mouse 5- hydroxytryptamine (1A) receptor ( 5- HT1A) receptors fused to the yellow fluorescent protein- and the cyan fluorescent protein ( CFP)- tagged alpha (i3) subunit of heterotrimeric G- protein to study spatiotemporal distribution of the 5- HT1Amediated signaling in living cells. We also addressed the question on the molecular mechanisms by which receptor palmitoylation may regulate communication between receptors and G i- proteins. Our data demonstrate that activation of the 5- HT1A receptor caused a partial release of G alpha(i) protein into the cytoplasm and that this translocation is accompanied by a significant increase of the intracellular Ca2+ concentration."],["dc.identifier.doi","10.1124/mol.107.037085"],["dc.identifier.isi","000248976400003"],["dc.identifier.pmid","17540717"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50651"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","0026-895X"],["dc.title","Localization of the mouse 5-Hydroxytryptamine(1A) receptor in lipid Microdomains depends on its palmitoylation and is involved in receptor-mediated signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3981"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","3992"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Bethani, Ioanna"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Geumann, Ulf"],["dc.contributor.author","Sieber, Jochen J."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:49:25Z"],["dc.date.available","2017-09-07T11:49:25Z"],["dc.date.issued","2007"],["dc.description.abstract","Soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins mediate organelle fusion in the secretory pathway. Different fusion steps are catalyzed by specific sets of SNARE proteins. Here we have used the SNAREs mediating the fusion of early endosomes and exocytosis, respectively, to investigate how pairing specificity is achieved. Although both sets of SNAREs promiscuously assemble in vitro, there is no functional crosstalk. We now show that they not only colocalize to overlapping microdomains in the membrane of early endosomes of neuroendocrine cells, but also form cis-complexes promiscuously, with the proportion of the different complexes being primarily dependent on mass action. Addition of soluble SNARE molecules onto native membranes revealed preference for cognate SNAREs. Furthermore, we found that SNAREs are laterally segregated at endosome contact sites, with the exocytotic synaptobrevin being depleted. We conclude that specificity in endosome fusion is mediated by the following two synergistically operating mechanisms: (i) preference for the cognate SNARE in 'trans' interactions and (ii) lateral segregation of SNAREs, leading to relative enrichment of the cognate ones at the prospective fusion sites."],["dc.identifier.doi","10.1038/sj.emboj.7601820"],["dc.identifier.gro","3143442"],["dc.identifier.isi","000249691800010"],["dc.identifier.pmid","17717530"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/956"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]