Milovanovic, Dragomir

[["dc.bibliographiccitation.artnumber","5984"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Koike, Seiichi"],["dc.contributor.author","Göttfert, Fabian"],["dc.contributor.author","Pähler, Gesa"],["dc.contributor.author","Junius, Meike"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Risselada, H. J."],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","The clustering of proteins and lipids in distinct microdomains is emerging as an important principle for the spatial patterning of biological membranes. Such domain formation can be the result of hydrophobic and ionic interactions with membrane lipids as well as of specific protein-protein interactions. Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismatch between the length of transmembrane domains (TMDs) and the thickness of the lipid membrane suffices to induce clustering of proteins. Even when the TMDs differ in length by only a single residue, hydrophobic mismatch can segregate structurally closely homologous membrane proteins in distinct membrane domains. Domain formation is further fine-tuned by interactions with polyanionic phosphoinositides and homo and heterotypic protein interactions. Our findings demonstrate that hydrophobic mismatch contributes to the structural organization of membranes."],["dc.identifier.doi","10.1038/ncomms6984"],["dc.identifier.fs","613597"],["dc.identifier.gro","3141986"],["dc.identifier.isi","000348812100002"],["dc.identifier.pmid","25635869"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13586"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3279"],["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","2041-1723"],["dc.rights.access","openAccess"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Fluorescence Resonance Energy Transfer"],["dc.subject.mesh","Fluorescent Antibody Technique"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Hydrophobic and Hydrophilic Interactions"],["dc.subject.mesh","Molecular Dynamics Simulation"],["dc.subject.mesh","Phosphatidylinositols"],["dc.subject.mesh","Protein Binding"],["dc.subject.mesh","Protein Structure, Tertiary"],["dc.subject.mesh","Rats"],["dc.subject.mesh","SNARE Proteins"],["dc.title","Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","12006"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Schwenen, Lando L. G."],["dc.contributor.author","Hubrich, Raphael"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Geil, Burkhard"],["dc.contributor.author","Yang, Jian"],["dc.contributor.author","Kros, Alexander"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:43:42Z"],["dc.date.available","2017-09-07T11:43:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Even though a number of different in vitro fusion assays have been developed to analyze protein mediated fusion, they still only partially capture the essential features of the in vivo situation. Here we established an in vitro fusion assay that mimics the fluidity and planar geometry of the cellular plasma membrane to be able to monitor fusion of single protein-containing vesicles. As a proof of concept, planar pore-spanning membranes harboring SNARE-proteins were generated on highly ordered functionalized 1.2 mu m-sized pore arrays in Si3N4. Full mobility of the membrane components was demonstrated by fluorescence correlation spectroscopy. Fusion was analyzed by two color confocal laser scanning fluorescence microscopy in a time resolved manner allowing to readily distinguish between vesicle docking, intermediate states such as hemifusion and full fusion. The importance of the membrane geometry on the fusion process was highlighted by comparing SNARE-mediated fusion with that of a minimal SNARE fusion mimetic."],["dc.identifier.doi","10.1038/srep12006"],["dc.identifier.fs","613746"],["dc.identifier.gro","3141864"],["dc.identifier.isi","000357847500001"],["dc.identifier.pmid","26165860"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13641"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1923"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 803, B04, B05]; Chinese Scholarship Council (CSC)"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2045-2322"],["dc.rights.access","openAccess"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Biomimetic Materials"],["dc.subject.mesh","Fluorescent Dyes"],["dc.subject.mesh","Gold"],["dc.subject.mesh","Kinetics"],["dc.subject.mesh","Membrane Fusion"],["dc.subject.mesh","Microscopy, Confocal"],["dc.subject.mesh","Models, Biological"],["dc.subject.mesh","Porosity"],["dc.subject.mesh","Rats"],["dc.subject.mesh","Recombinant Proteins"],["dc.subject.mesh","SNARE Proteins"],["dc.subject.mesh","Silicon Compounds"],["dc.subject.mesh","Time-Lapse Imaging"],["dc.subject.mesh","Unilamellar Liposomes"],["dc.title","Resolving single membrane fusion events on planar pore-spanning membranes"],["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"]]