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A minimalist model to measure interactions between proteins and synaptic vesicles

dc.contributor.authorPerego, Eleonora
dc.contributor.authorReshetniak, Sofiia
dc.contributor.authorLorenz, Charlotta
dc.contributor.authorHoffmann, Christian
dc.contributor.authorMilovanović, Dragomir
dc.contributor.authorRizzoli, Silvio O.
dc.contributor.authorKöster, Sarah
dc.date.accessioned2021-05-18T10:29:46Z
dc.date.available2021-05-18T10:29:46Z
dc.date.issued2020de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/17819
dc.description.abstractProtein dynamics in the synaptic bouton are still not well understood, despite many quantitative studies of synaptic structure and function. The complexity of the synaptic environment makes investigations of presynaptic protein mobility challenging. Here, we present an in vitro approach to create a minimalist model of the synaptic environment by patterning synaptic vesicles (SVs) on glass coverslips. We employed fluorescence correlation spectroscopy (FCS) to measure the mobility of monomeric enhanced green fluorescent protein (mEGFP)-tagged proteins in the presence of the vesicle patterns. We observed that the mobility of all eleven measured proteins is strongly reduced in the presence of the SVs, suggesting that they all bind to the SVs. The mobility observed in these conditions is within the range of corresponding measurements in synapses of living cells. Overall, our simple, but robust, approach should enable numerous future studies of organelle-protein interactions in general.de
dc.description.sponsorshipOpen-Access-Publikationsfonds 2020
dc.language.isoengde
dc.rightsopenAccess
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc530
dc.titleA minimalist model to measure interactions between proteins and synaptic vesiclesde
dc.typejournalArticlede
dc.identifier.doi10.1038/s41598-020-77887-1
dc.type.versionpublishedVersionde
dc.relation.eISSN2045-2322
dc.bibliographicCitation.volume10de
dc.bibliographicCitation.issue1de
dc.type.subtypejournalArticle
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalScientific Reportsde


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