Jahn, Reinhard

[["dc.bibliographiccitation.artnumber","012015"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Physics: Conference Series"],["dc.bibliographiccitation.volume","247"],["dc.contributor.affiliation","S Castorph, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.affiliation","L Arleth, ; 2Biophysics, Faculty of Life Sciences, University of Copenhagen, Frederiksberg, DK"],["dc.contributor.affiliation","M Sztucki, ; 3European Synchrotron Radiation Facility, Grenoble, F"],["dc.contributor.affiliation","U Vainio, ; 4Hamburger Synchrotronstrahlungslabor at Deutsches Elektronen-Synchrotron, Hamburg, D"],["dc.contributor.affiliation","S K Ghosh, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.affiliation","M Holt, ; 5Max Planck Institut für Biophysikalische Chemie, Department of Neurobiology, Göttingen, D"],["dc.contributor.affiliation","R Jahn, ; 5Max Planck Institut für Biophysikalische Chemie, Department of Neurobiology, Göttingen, D"],["dc.contributor.affiliation","T Salditt, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.author","Castorph, Simon"],["dc.contributor.author","Arleth, Lise"],["dc.contributor.author","Sztucki, Michael"],["dc.contributor.author","Vainio, Ulla"],["dc.contributor.author","Ghosh, S. K."],["dc.contributor.author","Holt, M."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:54:07Z"],["dc.date.available","2017-09-07T11:54:07Z"],["dc.date.issued","2010"],["dc.date.updated","2022-02-18T08:56:36Z"],["dc.description.abstract","We discuss different spherically symmetric and anisotropic form factor models and test them against high resolution synchrotron based small-angle x-ray scattering (SAXS) data from synaptic vesicles (SVs), isolated from rat brain. Anisotropy of the model form factors is found to be a key ingredient for the description of the native synaptic vesicle structure. We describe changes in structural parameters due to protease digestion of SVs, and present SAXS data of SVs recorded under different pH conditions."],["dc.identifier.doi","10.1088/1742-6596/247/1/012015"],["dc.identifier.fs","581310"],["dc.identifier.gro","3145120"],["dc.identifier.issn","1742-6596"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2821"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.relation.issn","1742-6596"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights.uri","https://publishingsupport.iopscience.iop.org/open_access/"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","neuro biophysics"],["dc.title","Synaptic Vesicles Studied by SAXS: Derivation and Validation of a Model Form Factor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","108623"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Cheret, Cyril"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Ahnert-Hilger, Gudrun"],["dc.date.accessioned","2021-04-14T08:30:33Z"],["dc.date.available","2021-04-14T08:30:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Vesicular glutamate transporters (VGLUTs) fill synaptic vesicles with glutamate. VGLUTs were originally identified as sodium-dependent transporters of inorganic phosphate (Pi), but the physiological relevance of this activity remains unclear. Heterologous expression of all three VGLUTs greatly augments intracellular Pi levels. Using neuronal models, we show that translocation of VGLUTs to the plasma membrane during exocytosis results in highly increased Pi uptake. VGLUT-mediated Pi influx is counteracted by Pi efflux. Synaptosomes prepared from perinatal VGLUT2−/− mice that are virtually free of VGLUTs show drastically reduced cytosolic Pi levels and fail to import Pi. Glutamate partially competes with sodium (Na+)/Pi (NaPi)-uptake mediated by VGLUTs but does not appear to be transported. A nanobody that blocks glutamate transport by binding to the cytoplasmic domain of VGLUT1 abolishes Pi transport when co-expressed with VGLUT1. We conclude that VGLUTs have a dual function that is essential for both vesicular glutamate loading and Pi restoration in neurons."],["dc.identifier.doi","10.1016/j.celrep.2020.108623"],["dc.identifier.pmid","33440152"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83282"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/232"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","2211-1247"],["dc.relation.workinggroup","RG Preobraschenski (Biochemistry of Membrane Dynamics)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Vesicular Glutamate Transporters (SLCA17 A6, 7, 8) Control Synaptic Phosphate Levels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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.journal","eLife"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Farsi, Zohreh"],["dc.contributor.author","Gowrisankaran, Sindhuja"],["dc.contributor.author","Krunic, Matija"],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Lafer, Eileen M"],["dc.contributor.author","Mim, Carsten"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Milosevic, Ira"],["dc.date.accessioned","2020-12-10T18:48:06Z"],["dc.date.available","2020-12-10T18:48:06Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.7554/eLife.32569"],["dc.identifier.eissn","2050-084X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15262"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79016"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2770"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","2776"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Wehland, Jan-Dirk"],["dc.contributor.author","Lygina, Antonina S."],["dc.contributor.author","Kumar, Pawan"],["dc.contributor.author","Guha, Samit"],["dc.contributor.author","Hubrich, Barbara E."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-01-23T14:36:40Z"],["dc.date.accessioned","2021-10-27T13:12:13Z"],["dc.date.available","2017-01-23T14:36:40Z"],["dc.date.available","2021-10-27T13:12:13Z"],["dc.date.issued","2016"],["dc.description.abstract","Fusion of synaptic vesicles with the presynaptic plasma membrane is mediated by Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor proteins also known as SNAREs. The backbone of this essential process is the assembly of SNAREs from opposite membranes into tight four helix bundles forcing membranes in close proximity. With model systems resembling SNAREs with reduced complexity we aim to understand how these proteins work at the molecular level. Here, peptide nucleic acids (PNAs) are used as excellent candidates for mimicking the SNARE recognition motif by forming well-characterized duplex structures. Hybridization between complementary PNA strands anchored in liposomes through native transmembrane domains (TMDs) induces the merger of the outer leaflets of the participating vesicles but not of the inner leaflets. A series of PNA/peptide hybrids differing in the length of TMDs and charges at the C-terminal end is presented. Interestingly, mixing of both outer and inner leaflets is seen for TMDs containing an amide in place of the natural carboxylic acid at the C-terminal end. Charged side chains at the C-terminal end of the TMDs are shown to have a negative impact on the mixing of liposomes. The length of the TMDs is vital for fusion as with the use of shortened TMDs, fusion was completely prevented."],["dc.identifier.doi","10.1039/C6MB00294C"],["dc.identifier.isi","000382253100010"],["dc.identifier.pmid","27345759"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14187"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91671"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1742-2051"],["dc.relation.issn","1742-206X"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","SNARE protein; peptide"],["dc.title","Role of the transmembrane domain in SNARE protein mediated membrane fusion: peptide nucleic acid/peptide model systems"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1908"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1920"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Salditt, Annalena"],["dc.contributor.author","Xu, Yihui"],["dc.contributor.author","Yavuz, Halenur"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2020-03-03T08:17:24Z"],["dc.date.available","2020-03-03T08:17:24Z"],["dc.date.issued","2018"],["dc.description.abstract","We have studied the adhesion state (also denoted by docking state) of lipid vesicles as induced by the divalent ions Ca2+ or Mg2+ at well-controlled ion concentration, lipid composition, and charge density. The bilayer structure and the interbilayer distance in the docking state were analyzed by small-angle x-ray scattering. A strong adhesion state was observed for DOPC:DOPS vesicles, indicating like-charge attraction resulting from ion correlations. The observed interbilayer separations of ∼1.6 nm agree quantitatively with the predictions of electrostatics in the strong coupling regime. Although this phenomenon was observed when mixing anionic and zwitterionic (or neutral) lipids, pure anionic membranes (DOPS) with highest charge density σ resulted in a direct phase transition to a multilamellar state, which must be accompanied by rupture and fusion of vesicles. To extend the structural assay toward protein-controlled docking and fusion, we have characterized reconstituted N-ethylmaleimide-sensitive factor attachment protein receptors in controlled proteoliposome suspensions by small-angle x-ray scattering."],["dc.identifier.doi","10.1016/j.bpj.2018.02.040"],["dc.identifier.pmid","29694868"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63067"],["dc.language.iso","en"],["dc.relation.eissn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Vesicle Adhesion and Fusion Studied by Small-Angle X-Ray Scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","105004"],["dc.bibliographiccitation.journal","New Journal of Physics"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Ghosh, S. K."],["dc.contributor.author","Castorph, S."],["dc.contributor.author","Konovalov, O."],["dc.contributor.author","Jahn, R."],["dc.contributor.author","Holt, M."],["dc.contributor.author","Salditt, T."],["dc.date.accessioned","2017-09-07T11:45:15Z"],["dc.date.available","2017-09-07T11:45:15Z"],["dc.date.issued","2010"],["dc.description.abstract","The fusion of synaptic vesicles (SVs) with the plasma membrane in neurons is a crucial step in the release of neurotransmitters, which are responsible for carrying signals between nerve cells. While many of the molecular players involved in this fusion process have been identified, a precise molecular description of their roles in the process is still lacking. A case in point is the plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2). Although PIP2 is known to be essential for vesicle fusion, its precise role in the process remains unclear. We have re-investigated the role of this lipid in membrane structure and function using the complementary experimental techniques of x-ray reflectivity, both on lipid monolayers at an air-water interface and bilayers on a solid support, and grazing incidence x-ray diffraction on lipid monolayers. These techniques provide unprecedented access to structural information at the molecular level, and detail the profound structural changes that occur in a membrane following PIP2 incorporation. Further, we also confirm and extend previous findings that the association of SVs with membranes is enhanced by PIP2 incorporation, and reveal the structural changes that underpin this phenomenon. Further, the association is further intensified by a physiologically relevant amount of Ca2+ ions in the subphase of the monolayer, as revealed by the increase in interfacial pressure seen with the lipid monolayer system. Finally, a theoretical calculation concerning the products arising from the fusion of these SVs with proteoliposomes is presented, with which we aim to illustrate the potential future uses of this system."],["dc.identifier.doi","10.1088/1367-2630/12/10/105004"],["dc.identifier.fs","572802"],["dc.identifier.gro","3142842"],["dc.identifier.isi","000284768300002"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7194"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/290"],["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","1367-2630"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","membrane biophysics"],["dc.subject.gro","neuro biophysics"],["dc.title","In vitro study of interaction of synaptic vesicles with lipid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","63"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The European Physical Journal E"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Castorph, S."],["dc.contributor.author","Schwarz Henriques, S."],["dc.contributor.author","Holt, M."],["dc.contributor.author","Riedel, D."],["dc.contributor.author","Jahn, R."],["dc.contributor.author","Salditt, T."],["dc.date.accessioned","2017-09-07T11:44:14Z"],["dc.date.available","2017-09-07T11:44:14Z"],["dc.date.issued","2011"],["dc.description.abstract","The size polydispersity distribution of synaptic vesicles (SVs) is characterized under quasi-physiological conditions by dynamic light scattering (DLS). Highly purified fractions of SVs obtained from rat brain still contain a small amount of larger contaminant structures, which can be quantified by DLS and further reduced by asymmetric-flow field-flow (AFFF) fractionation. The intensity autocorrelation functions g(2)(tau) recorded from these samples are analyzed by a constrained regularization method as well as by an alternative direct modeling approach. The results are in quantitative agreement with the polydispersity obtained from cryogenic electron microscopy of vitrified SVs. Next, different vesicle fusion assays based on samples composed of SVs and small unilamellar proteoliposomes with the fusion proteins syntaxin 1 and SNAP-25A are characterized by DLS. The size increase of the proteoliposomes due to SNARE-dependent fusion with SVs is quantified by DLS under quasi-physiological conditions."],["dc.identifier.doi","10.1140/epje/i2011-11063-2"],["dc.identifier.gro","3142718"],["dc.identifier.isi","000292512700001"],["dc.identifier.pmid","21706281"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7576"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/153"],["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","1292-8941"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","neuro biophysics"],["dc.title","Synaptic vesicles studied by dynamic light scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["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"]]