Risselada, Herre Jelger

[["dc.bibliographiccitation.firstpage","552"],["dc.bibliographiccitation.issue","7374"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","555"],["dc.bibliographiccitation.volume","479"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Amin, Hayder"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Hubrich, Barbara E."],["dc.contributor.author","Dier, Markus"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2011"],["dc.description.abstract","Neuronal exocytosis is catalysed by the SNAP receptor protein syntaxin-1A(1), which is clustered in the plasma membrane at sites where synaptic vesicles undergo exocytosis(2,3). However, how syntaxin-1A is sequestered is unknown. Here we show that syntaxin clustering is mediated by electrostatic interactions with the strongly anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2). Using super-resolution stimulated-emission depletion microscopy on the plasma membranes of PC12 cells, we found that PIP2 is the dominant inner-leaflet lipid in microdomains about 73 nanometres in size. This high accumulation of PIP2 was required for syntaxin-1A sequestering, as destruction of PIP2 by the phosphatase synaptojanin-1 reduced syntaxin-1A clustering. Furthermore, coreconstitution of PIP2 and the carboxy-terminal part of syntaxin-1A in artificial giant unilamellar vesicles resulted in segregation of PIP2 and syntaxin-1A into distinct domains even when cholesterol was absent. Our results demonstrate that electrostatic protein-lipid interactions can result in the formation of microdomains independently of cholesterol or lipid phases."],["dc.identifier.doi","10.1038/nature10545"],["dc.identifier.gro","3142626"],["dc.identifier.isi","000297285600056"],["dc.identifier.pmid","22020284"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51"],["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","0028-0836"],["dc.title","Membrane protein sequestering by ionic protein-lipid interactions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","805"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U82"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Thutupalli, Shashi"],["dc.contributor.author","Risselada, J. H."],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Herminghaus, Stephan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:10Z"],["dc.date.available","2017-09-07T11:44:10Z"],["dc.date.issued","2011"],["dc.description.abstract","Synaptotagmin-1 triggers Ca2+-sensitive, rapid neurotransmitter release by promoting interactions between SNARE proteins on synaptic vesicles and the plasma membrane. How synaptotagmin-1 promotes this interaction is unclear, and the massive increase in membrane fusion efficiency of Ca2+-bound synaptotagmin-1 has not been reproduced in vitro. However, previous experiments have been performed at relatively high salt concentrations, screening potentially important electrostatic interactions. Using functional reconstitution in liposomes, we show here that at low ionic strength SNARE-mediated membrane fusion becomes strictly dependent on both Ca2+ and synaptotagmin-1. Under these conditions, synaptotagmin-1 functions as a distance regulator that tethers the liposomes too far from the plasma membrane for SNARE nucleation in the absence of Ca2+, but while bringing the liposomes close enough for membrane fusion in the presence of Ca2+. These results may explain how the relatively weak electrostatic interactions between synaptotagmin-1 and membranes substantially accelerate fusion."],["dc.identifier.doi","10.1038/nsmb.2061"],["dc.identifier.gro","3142704"],["dc.identifier.isi","000292507500009"],["dc.identifier.pmid","21642968"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/138"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9993"],["dc.title","Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","679"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","686"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Iraheta, Emilio"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Mueller, Veronika"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Fasshauer, Dirk"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Kühnel, Karin"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:47:41Z"],["dc.date.available","2017-09-07T11:47:41Z"],["dc.date.issued","2013"],["dc.description.abstract","Synaptic-vesicle exocytosis is mediated by the vesicular Ca2+ sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca2+ through PIP2. This interaction allows both Ca2+-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca2+ triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca2+ influx bringing the vesicle membrane close enough for membrane fusion."],["dc.identifier.doi","10.1038/nsmb.2570"],["dc.identifier.gro","3142345"],["dc.identifier.isi","000319915900008"],["dc.identifier.pmid","23665582"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7253"],["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","1545-9993"],["dc.title","Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["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.firstpage","343001"],["dc.bibliographiccitation.issue","34"],["dc.bibliographiccitation.journal","Journal of Physics. D, Applied Physics"],["dc.bibliographiccitation.volume","51"],["dc.contributor.affiliation","Bassereau, Patricia;"],["dc.contributor.affiliation","Jin, Rui;"],["dc.contributor.affiliation","Baumgart, Tobias;"],["dc.contributor.affiliation","Deserno, Markus;"],["dc.contributor.affiliation","Dimova, Rumiana;"],["dc.contributor.affiliation","Frolov, Vadim A;"],["dc.contributor.affiliation","Bashkirov, Pavel V;"],["dc.contributor.affiliation","Grubmüller, Helmut;"],["dc.contributor.affiliation","Jahn, Reinhard;"],["dc.contributor.affiliation","Risselada, H Jelger;"],["dc.contributor.affiliation","Johannes, Ludger;"],["dc.contributor.affiliation","Kozlov, Michael M;"],["dc.contributor.affiliation","Lipowsky, Reinhard;"],["dc.contributor.affiliation","Pucadyil, Thomas J;"],["dc.contributor.affiliation","Zeno, Wade F;"],["dc.contributor.affiliation","Stachowiak, Jeanne C;"],["dc.contributor.affiliation","Stamou, Dimitrios;"],["dc.contributor.affiliation","Breuer, Artù;"],["dc.contributor.affiliation","Lauritsen, Line;"],["dc.contributor.affiliation","Simon, Camille;"],["dc.contributor.affiliation","Sykes, Cécile;"],["dc.contributor.affiliation","Voth, Gregory A;"],["dc.contributor.affiliation","Weikl, Thomas R;"],["dc.contributor.author","Bassereau, Patricia"],["dc.contributor.author","Jin, Rui"],["dc.contributor.author","Baumgart, Tobias"],["dc.contributor.author","Deserno, Markus"],["dc.contributor.author","Dimova, Rumiana"],["dc.contributor.author","Frolov, Vadim A"],["dc.contributor.author","Bashkirov, Pavel V"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Johannes, Ludger"],["dc.contributor.author","Kozlov, Michael M."],["dc.contributor.author","Lipowsky, Reinhard"],["dc.contributor.author","Pucadyil, Thomas J."],["dc.contributor.author","Zeno, Wade F."],["dc.contributor.author","Stachowiak, Jeanne C."],["dc.contributor.author","Stamou, Dimitrios"],["dc.contributor.author","Breuer, Artù"],["dc.contributor.author","Lauritsen, Line"],["dc.contributor.author","Simon, Camille"],["dc.contributor.author","Sykes, Cécile"],["dc.contributor.author","Voth, Gregory A."],["dc.contributor.author","Weikl, Thomas R."],["dc.date.accessioned","2020-12-10T18:15:41Z"],["dc.date.available","2020-12-10T18:15:41Z"],["dc.date.issued","2018"],["dc.date.updated","2022-02-09T13:18:50Z"],["dc.description.abstract","Abstract The importance of curvature as a structural feature of biological membranes has been recognized for many years and has fascinated scientists from a wide range of different backgrounds. On the one hand, changes in membrane morphology are involved in a plethora of phenomena involving the plasma membrane of eukaryotic cells, including endo- and exocytosis, phagocytosis and filopodia formation. On the other hand, a multitude of intracellular processes at the level of organelles rely on generation, modulation, and maintenance of membrane curvature to maintain the organelle shape and functionality. The contribution of biophysicists and biologists is essential for shedding light on the mechanistic understanding and quantification of these processes. Given the vast complexity of phenomena and mechanisms involved in the coupling between membrane shape and function, it is not always clear in what direction to advance to eventually arrive at an exhaustive understanding of this important research area. The 2018 Biomembrane Curvature and Remodeling Roadmap of Journal of Physics D: Applied Physics addresses this need for clarity and is intended to provide guidance both for students who have just entered the field as well as established scientists who would like to improve their orientation within this fascinating area."],["dc.identifier.doi","10.1088/1361-6463/aacb98"],["dc.identifier.eissn","1361-6463"],["dc.identifier.issn","0022-3727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74924"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","IOP Publishing"],["dc.rights.uri","http://creativecommons.org/licenses/by/3.0/"],["dc.title","The 2018 biomembrane curvature and remodeling roadmap"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]