Jahn, Reinhard

[["dc.bibliographiccitation.firstpage","465"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","482"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Alfken, Jette"],["dc.contributor.author","Neuhaus, Charlotte"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2022-09-01T09:51:27Z"],["dc.date.available","2022-09-01T09:51:27Z"],["dc.date.issued","2022-07-29"],["dc.description.abstract","The size, polydispersity, and electron density profile of synaptic vesicles (SVs) can be studied by small-angle X-ray scattering (SAXS), i.e. by X-ray diffraction from purified SV suspensions in solution. Here we show that size and shape transformations, as they appear in the functional context of these important synaptic organelles, can also be monitored by SAXS. In particular, we have investigated the active uptake of neurotransmitters, and find a mean vesicle radius increase of about 12% after the uptake of glutamate, which indicates an unusually large extensibility of the vesicle surface, likely to be accompanied by conformational changes of membrane proteins and rearrangements of the bilayer. Changes in the electron density profile (EDP) give first indications for such a rearrangement. Details of the protein structure are screened, however, by SVs polydispersity. To overcome the limitations of large ensemble averages and heterogeneous structures, we therefore propose serial X-ray diffraction by single free electron laser pulses. Using simulated data for realistic parameters, we show that this is in principle feasible, and that even spatial distances between vesicle proteins could be assessed by this approach."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Georg-August-Universität Göttingen 501100003385"],["dc.identifier.doi","10.1007/s00249-022-01609-w"],["dc.identifier.pii","1609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113969"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.gro","Synaptic vesicle"],["dc.subject.gro","Small angle X-ray scattering"],["dc.subject.gro","Neurotransmitter uptake"],["dc.subject.gro","Synchrotron and free electron laser techniques"],["dc.title","Neurotransmitter uptake of synaptic vesicles studied by X-ray diffraction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.artnumber","7540"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Birinci, Yelda"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Park, Yongsoo"],["dc.date.accessioned","2022-11-02T09:17:09Z"],["dc.date.available","2022-11-02T09:17:09Z"],["dc.date.issued","2020"],["dc.description.abstract","Large dense-core vesicles (LDCVs) contain a variety of neurotransmitters, proteins, and hormones such as biogenic amines and peptides, together with microRNAs (miRNAs). Isolation of LDCVs is essential for functional studies including vesicle fusion, vesicle acidification, monoamine transport, and the miRNAs stored in LDCVs. Although several methods were reported for purifying LDCVs, the final fractions are significantly contaminated by other organelles, compromising biochemical characterization. Here we isolated LDCVs (chromaffin granules) with high yield and purity from bovine adrenal medulla. The fractionation protocol combines differential and continuous sucrose gradient centrifugation, allowing for reducing major contaminants such as mitochondria. Purified LDCVs show robust acidification by the endogenous V-ATPase and undergo SNARE-mediated fusion with artificial membranes. Interestingly, LDCVs contain specific miRNAs such as miR-375 and miR-375 is stabilized by protein complex against RNase A. This protocol can be useful in research on the biological functions of LDCVs."],["dc.identifier.doi","10.1038/s41598-020-64486-3"],["dc.identifier.pmid","32371955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116909"],["dc.language.iso","en"],["dc.relation.haserratum","/handle/2/116642"],["dc.relation.issn","2045-2322"],["dc.title","Isolation of large dense-core vesicles from bovine adrenal medulla for functional studies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3904"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Kreutzberger, Alex J. B."],["dc.contributor.author","Kiessling, Volker"],["dc.contributor.author","Stroupe, Christopher"],["dc.contributor.author","Liang, Binyong"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Kreutzberger, Mark A. B."],["dc.contributor.author","Nakamoto, Robert"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Castle, J. David"],["dc.contributor.author","Tamm, Lukas K."],["dc.date.accessioned","2019-12-03T14:41:08Z"],["dc.date.available","2019-12-03T14:41:08Z"],["dc.date.issued","2019"],["dc.description.abstract","Regulated exocytosis of synaptic vesicles is substantially faster than of endocrine dense core vesicles despite similar molecular machineries. The reasons for this difference are unknown and could be due to different regulatory proteins, different spatial arrangements, different vesicle sizes, or other factors. To address these questions, we take a reconstitution approach and compare regulated SNARE-mediated fusion of purified synaptic and dense core chromaffin and insulin vesicles using a single vesicle-supported membrane fusion assay. In all cases, Munc18 and complexin are required to restrict fusion in the absence of calcium. Calcium triggers fusion of all docked vesicles. Munc13 (C1C2MUN domain) is required for synaptic and enhanced insulin vesicle fusion, but not for chromaffin vesicles, correlating inversely with the presence of CAPS protein on purified vesicles. Striking disparities in calcium-triggered fusion rates are observed, increasing with curvature with time constants 0.23 s (synaptic vesicles), 3.3 s (chromaffin vesicles), and 9.1 s (insulin vesicles) and correlating with rate differences in cells."],["dc.identifier.doi","10.1038/s41467-019-11873-8"],["dc.identifier.pmid","31467284"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62722"],["dc.language.iso","en"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.title","In vitro fusion of single synaptic and dense core vesicles reproduces key physiological properties"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Birinci, Yelda"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Park, Yongsoo"],["dc.date.accessioned","2022-11-01T10:16:45Z"],["dc.date.available","2022-11-01T10:16:45Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1038/s41598-022-21361-7"],["dc.identifier.pii","21361"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116642"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-605"],["dc.relation.eissn","2045-2322"],["dc.relation.iserratumof","/handle/2/116909"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Author Correction: Isolation of large dense-core vesicles from bovine adrenal medulla for functional studies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]