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Antibody-driven capture of synaptic vesicle proteins on the plasma membrane enables the analysis of their interactions with other synaptic proteins

dc.contributor.authorRichter, Katharina N.
dc.contributor.authorPatzelt, Christina
dc.contributor.authorPhan, Nhu T. N.
dc.contributor.authorRizzoli, Silvio O.
dc.date.accessioned2019-08-07T12:38:49Z
dc.date.available2019-08-07T12:38:49Z
dc.date.issued2019de
dc.relation.ISSN2045-2322de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/16340
dc.description.abstractMany organelles from the secretory pathway fuse to the plasma membrane, to exocytose different cargoes. Their proteins are then retrieved from the plasma membrane by endocytosis, and the organelles are re-formed. It is generally unclear whether the organelle proteins colocalize when they are on the plasma membrane, or whether they disperse. To address this, we generated here a new approach, which we tested on synaptic vesicles, organelles that are known to exo- and endocytose frequently. We tagged the synaptotagmin molecules of newly exocytosed vesicles using clusters of primary and secondary antibodies targeted against the luminal domains of these molecules. The antibody clusters are too large for endocytosis, and thus sequestered the synaptotagmin molecules on the plasma membrane. Immunostainings for other synaptic molecules then revealed whether they colocalized with the sequestered synaptotagmin molecules. We suggest that such assays may be in the future extended to other cell types and other organelles.de
dc.language.isoengde
dc.rightsopenAccess
dc.rights.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/16340
dc.subjectsynaptic proteins; Antibody-driven capture; plasma membranede
dc.subject.ddc006
dc.subject.ddc573
dc.subject.ddc612
dc.titleAntibody-driven capture of synaptic vesicle proteins on the plasma membrane enables the analysis of their interactions with other synaptic proteinsde
dc.typejournalArticlede
dc.identifier.doi10.1038/s41598-019-45729-4
dc.type.versionpublishedVersionde
dc.relation.eISSN2045-2322
dc.bibliographicCitation.volume9de
dc.bibliographicCitation.issue1de
dc.type.subtypejournalArticle
dc.identifier.pmid31239503
dc.bibliographicCitation.articlenumber9231de
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalScientific Reportsde


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