Preobraschenski, Julia

[["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.firstpage","827"],["dc.bibliographiccitation.issue","7937"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","834"],["dc.bibliographiccitation.volume","611"],["dc.contributor.author","Kosmidis, Eleftherios"],["dc.contributor.author","Shuttle, Christopher G."],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Johnson, Peter J."],["dc.contributor.author","Veshaguri, Salome"],["dc.contributor.author","Holmkvist, Jesper"],["dc.contributor.author","Møller, Mads P."],["dc.contributor.author","Marantos, Orestis"],["dc.contributor.author","Marcoline, Frank"],["dc.contributor.author","Stamou, Dimitrios"],["dc.date.accessioned","2022-12-01T08:30:53Z"],["dc.date.available","2022-12-01T08:30:53Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1038/s41586-022-05472-9"],["dc.identifier.pii","5472"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118007"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.rights.uri","https://www.springer.com/tdm"],["dc.title","Regulation of the mammalian-brain V-ATPase through ultraslow mode-switching"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kreutzberger, Alex J. B."],["dc.contributor.author","Kiessling, Volker"],["dc.contributor.author","Doyle, Catherine A."],["dc.contributor.author","Schenk, Noah"],["dc.contributor.author","Upchurch, Clint M."],["dc.contributor.author","Elmer-Dixon, Margaret"],["dc.contributor.author","Ward, Amanda E."],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Hussein, Syed S."],["dc.contributor.author","Tomaka, Weronika"],["dc.contributor.author","Seelheim, Patrick"],["dc.contributor.author","Kattan, Iman"],["dc.contributor.author","Harris, Megan"],["dc.contributor.author","Liang, Binyong"],["dc.contributor.author","Kenworthy, Anne K."],["dc.contributor.author","Desai, Bimal N."],["dc.contributor.author","Leitinger, Norbert"],["dc.contributor.author","Anantharam, Arun"],["dc.contributor.author","Castle, J. David"],["dc.contributor.author","Tamm, Lukas K."],["dc.date.accessioned","2021-04-14T08:31:01Z"],["dc.date.available","2021-04-14T08:31:01Z"],["dc.date.issued","2020"],["dc.description.abstract","Insulin secretion from β-cells is reduced at the onset of type-1 and during type-2 diabetes. Although inflammation and metabolic dysfunction of β-cells elicit secretory defects associated with type-1 or type-2 diabetes, accompanying changes to insulin granules have not been established. To address this, we performed detailed functional analyses of insulin granules purified from cells subjected to model treatments that mimic type-1 and type-2 diabetic conditions and discovered striking shifts in calcium affinities and fusion characteristics. We show that this behavior is correlated with two subpopulations of insulin granules whose relative abundance is differentially shifted depending on diabetic model condition. The two types of granules have different release characteristics, distinct lipid and protein compositions, and package different secretory contents alongside insulin. This complexity of β-cell secretory physiology establishes a direct link between granule subpopulation and type of diabetes and leads to a revised model of secretory changes in the diabetogenic process."],["dc.identifier.doi","10.7554/eLife.62506"],["dc.identifier.pmid","33164744"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83454"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/143"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2050-084X"],["dc.relation.workinggroup","RG Preobraschenski (Biochemistry of Membrane Dynamics)"],["dc.rights","CC BY 4.0"],["dc.title","Distinct insulin granule subpopulations implicated in the secretory pathology of diabetes types 1 and 2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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"]]