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Title: The bruchpilot cytomatrix determines the size of the readily releasable pool of synaptic vesicles
Authors: Matkovic, TanjaSiebert, MatthiasKnoche, ElenaDepner, HaraldMertel, SaraOwald, DavidSchmidt, ManuelaThomas, UlrichSickmann, AlbertKamin, DirkHell, Stefan W.Bürger, JörgHollmann, ChristinaMielke, ThorstenWichmann, CarolinSigrist, Stephan J.
Publishers Version: https://doi.org/10.1083/jcb.201301072
Issue Date: 2013
Published in: Journal of Cell Biology, Volume 202, Issue 4, Page 667-683
Publisher: London : Nature Publishing Group
Abstract: Synaptic 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.
Keywords: Bruchpilot protein; calcium channel; Drosophila protein; unclassified drug
DDC: 570
License: CC BY-NC-SA 3.0 Unported
Link to License: https://creativecommons.org/licenses/by-nc-sa/3.0/
Appears in Collections:Biowissenschaften



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