Lang, Thorsten

[["dc.bibliographiccitation.firstpage","394"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","404"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Halemani, Nagaraj D."],["dc.contributor.author","Bethani, Ioanna"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lang, Thorsten"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","SNAREs are clustered membrane proteins essential for intracellular fusion steps. During fusion, three to four SNAREs with a Q(a)-, Q(b)-, Q(c)- and R-SNARE-motif form a complex. The core complex represents a Q(a)Q(b)Q(c)R-SNARE-motif bundle, most certainly assembling in steps. However, to date it is unknown which intermediate SNARE complex observed in vitro also exists in vivo. Here we have applied comparative fluorescence recovery after photobleaching (FRAP)-studies as a novel approach for studying in intact cells a SNARE interaction involved in synaptic vesicle fusion [catalyzed by syntaxin 1A (Q(a)), SNAP25 (Q(b)/Q(c)) and synaptobrevin 2 (R)]. We find that the Q(b)-SNARE-motif of SNAP25 interacts reversibly with clustered syntaxin. The interaction requires most of the alpha helical Q(b)-SNARE-motif and depends on its position within the molecule. We conclude that a zippered Q(a)Q(b)-SNARE complex represents a short-lived SNARE intermediate in intact cells, most likely providing an initial molecular platform toward membrane fusion."],["dc.identifier.doi","10.1111/j.1600-0854.2009.01020.x"],["dc.identifier.gro","3142960"],["dc.identifier.isi","000274454500008"],["dc.identifier.pmid","20002656"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/421"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [LA1272/2-3]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","1398-9219"],["dc.title","Structure and Dynamics of a Two-Helix SNARE Complex in Live Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","116"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Physiology"],["dc.bibliographiccitation.lastpage","124"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Fluorescence microscopy is powerful for analyzing the composition and dynamics of cellular elements, but studying precise molecule patterns is precluded due to diffraction limited resolution. This barrier has been lifted now through several superresolution microscopy techniques. They revealed that proteins assemble in defined groups (clusters). A new challenge thus appears for the biologist: to find out whether clusters are molecular machines, stabilizers of defined protein conformations, or simply protein reservoirs."],["dc.identifier.doi","10.1152/physiol.00044.2009"],["dc.identifier.gro","3142947"],["dc.identifier.isi","000278117100006"],["dc.identifier.pmid","20430955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/407"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1548-9213"],["dc.title","Membrane Protein Clusters at Nanoscale Resolution: More Than Pretty Pictures"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","4509"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Saka, Sinem K."],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Lang, Thorsten"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:46:11Z"],["dc.date.available","2017-09-07T11:46:11Z"],["dc.date.issued","2014"],["dc.description.abstract","Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter hypothesis has been difficult to test in the past. Here, we introduce several approaches based on click chemistry, through which we study the distribution of membrane proteins in living cells, as well as in membrane sheets. We found that the plasma membrane proteins form multi-protein assemblies that are long lived (minutes), and in which protein diffusion is restricted. The formation of the assemblies is dependent on cholesterol. They are separated and anchored by the actin cytoskeleton. Specific proteins are preferentially located in different regions of the assemblies, from their cores to their edges. We conclude that the assemblies constitute a basic mesoscale feature of the membrane, which affects the patterning of most membrane proteins, and possibly also their activity."],["dc.identifier.doi","10.1038/ncomms5509"],["dc.identifier.gro","3142092"],["dc.identifier.isi","000340625100012"],["dc.identifier.pmid","25060237"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10970"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4456"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","Multi-protein assemblies underlie the mesoscale organization of the plasma membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["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","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"]]