The bruchpilot cytomatrix determines the size of the readily releasable pool of synaptic vesicles

dc.bibliographicCitation.firstPage667
dc.bibliographicCitation.issue4eng
dc.bibliographicCitation.lastPage683
dc.bibliographicCitation.volume202
dc.contributor.authorMatkovic, Tanja
dc.contributor.authorSiebert, Matthias
dc.contributor.authorKnoche, Elena
dc.contributor.authorDepner, Harald
dc.contributor.authorMertel, Sara
dc.contributor.authorOwald, David
dc.contributor.authorSchmidt, Manuela
dc.contributor.authorThomas, Ulrich
dc.contributor.authorSickmann, Albert
dc.contributor.authorKamin, Dirk
dc.contributor.authorHell, Stefan W.
dc.contributor.authorBürger, Jörg
dc.contributor.authorHollmann, Christina
dc.contributor.authorMielke, Thorsten
dc.contributor.authorWichmann, Carolin
dc.contributor.authorSigrist, Stephan J.
dc.date.accessioned2018-02-19T22:04:28Z
dc.date.available2019-06-18T09:00:55Z
dc.date.issued2013
dc.description.abstractSynaptic vesicles (SVs) fuse at a specialized membrane domain called the active zone (AZ), covered by a conserved cytomatrix. How exactly cytomatrix components intersect with SV release remains insufficiently understood. We showed previously that loss of the Drosophila melanogaster ELKS family protein Bruchpilot (BRP) eliminates the cytomatrix (T bar) and declusters Ca2+ channels. In this paper, we explored additional functions of the cytomatrix, starting with the biochemical identification of two BRP isoforms. Both isoforms alternated in a circular array and were important for proper T-bar formation. Basal transmission was decreased in isoform-specific mutants, which we attributed to a reduction in the size of the readily releasable pool (RRP) of SVs. We also found a corresponding reduction in the number of SVs docked close to the remaining cytomatrix. We propose that the macromolecular architecture created by the alternating pattern of the BRP isoforms determines the number of Ca2+ channel-coupled SV release slots available per AZ and thereby sets the size of the RRP.eng
dc.description.versionpublishedVersioneng
dc.formatapplication/pdf
dc.identifier.urihttps://doi.org/10.34657/470
dc.identifier.urihttps://oa.tib.eu/renate/handle/123456789/26
dc.language.isoengeng
dc.publisherLondon : Nature Publishing Groupeng
dc.relation.doihttps://doi.org/10.1083/jcb.201301072
dc.relation.ispartofseriesJournal of Cell Biology, Volume 202, Issue 4, Page 667-683eng
dc.rights.licenseCC BY-NC-SA 3.0 Unportedeng
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/3.0/eng
dc.subjectBruchpilot proteineng
dc.subjectcalcium channeleng
dc.subjectDrosophila proteineng
dc.subjectunclassified drugeng
dc.subject.ddc570eng
dc.titleThe bruchpilot cytomatrix determines the size of the readily releasable pool of synaptic vesicleseng
dc.typearticleeng
dc.typeTexteng
dcterms.bibliographicCitation.journalTitleJournal of Cell Biologyeng
tib.accessRightsopenAccesseng
wgl.contributorLINeng
wgl.contributorISASeng
wgl.subjectBiowissenschaften/Biologieeng
wgl.typeZeitschriftenartikeleng
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