Preobraschenski, Julia

[["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.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"]]