Diederichsen, Ulf

[["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","S31"],["dc.bibliographiccitation.journal","Journal of Peptide Science"],["dc.bibliographiccitation.lastpage","S32"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Lygina, Antonina S."],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T09:06:40Z"],["dc.date.available","2018-11-07T09:06:40Z"],["dc.date.issued","2012"],["dc.identifier.isi","000308091500035"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25608"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1075-2617"],["dc.title","SNARE analogous peptides for membrane fusion"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.firstpage","16447"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","16453"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2018-11-07T09:10:27Z"],["dc.date.available","2018-11-07T09:10:27Z"],["dc.date.issued","2012"],["dc.description.abstract","Synaptotagmin-1 is the main Ca2+ sensor of neuronal exocytosis. It binds to both Ca2+ and the anionic phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2), but the precise cooperativity of this binding is still poorly understood. Here, we used microscale thermophoresis to quantify the cooperative binding of PIP2 and Ca2+ to synaptotagmin-1. We found that PIP2 bound to the well conserved polybasic patch of the C2B domain with an apparent dissociation constant of similar to 20 mu M. PIP2 binding reduced the apparent dissociation constant for Ca2+ from similar to 250 to <5 mu M. Thus, our data show that PIP2 makes synaptotagmin-1 >40-fold more sensitive to Ca2+. This interplay between Ca2+, synaptotagmin-1, and PIP2 is crucial for neurotransmitter release."],["dc.identifier.doi","10.1074/jbc.M112.343418"],["dc.identifier.isi","000304030900035"],["dc.identifier.pmid","22447935"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26494"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Phosphatidylinositol 4,5-Bisphosphate Increases Ca2+ Affinity of Synaptotagmin-1 by 40-fold"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9405"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Chemical Communications"],["dc.bibliographiccitation.lastpage","9407"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Lygina, Antonina S."],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2019-07-09T11:54:16Z"],["dc.date.available","2019-07-09T11:54:16Z"],["dc.date.issued","2011"],["dc.description.abstract","SNARE proteins mediate membrane fusion between synaptic vesicles and the plasma membrane. A minimized peptide SNARE model system with reduced complexity was introduced combining the native SNARE transmembrane (TMD) and linker domains with artificial coiled-coil forming peptides. Specific membrane fusion initiated by coiled-coil recognition was shown by lipid and content mixing vesicle assays."],["dc.identifier.doi","10.1039/c1cc12879e"],["dc.identifier.fs","578739"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8676"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60607"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1364-548X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","SNARE derived peptide mimic inducing membrane fusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7868"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","7876"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Junius, Meike"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","van den Bogaart, Geert"],["dc.date.accessioned","2020-12-10T18:12:56Z"],["dc.date.available","2020-12-10T18:12:56Z"],["dc.date.issued","2016"],["dc.description.abstract","Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form domains in the plasma membrane that constitute recognition sites for vesicle docking. Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the molecular mechanism was unknown. Here, using a combination of superresolution stimulated emission depletion microscopy, FRET, and atomic force microscopy, we show that Ca(2+)acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/PI(4,5)P2complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological Ca(2+)concentrations is likely to be important for Ca(2+)-regulated secretion."],["dc.identifier.doi","10.1074/jbc.M116.716225"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","26884341"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74536"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.relation.eissn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.title","Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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","160"],["dc.bibliographiccitation.journal","iScience"],["dc.bibliographiccitation.lastpage","177"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Baranov, Maksim V."],["dc.contributor.author","Bianchi, Frans"],["dc.contributor.author","Schirmacher, Anastasiya"],["dc.contributor.author","van Aart, Melissa A. C."],["dc.contributor.author","Maassen, Sjors"],["dc.contributor.author","Muntjewerff, Elke M."],["dc.contributor.author","Dingjan, Ilse"],["dc.contributor.author","ter Beest, Martin"],["dc.contributor.author","Verdoes, Martijn"],["dc.contributor.author","Keyser, Samantha G. L."],["dc.contributor.author","Bertozzi, Carolyn R."],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","van den Bogaart, Geert"],["dc.date.accessioned","2020-12-10T14:24:42Z"],["dc.date.available","2020-12-10T14:24:42Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.isci.2018.12.015"],["dc.identifier.issn","2589-0042"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72327"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The Phosphoinositide Kinase PIKfyve Promotes Cathepsin-S-Mediated Major Histocompatibility Complex Class II Antigen Presentation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]