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  Active zone scaffolds differentially accumulate Unc13 isoforms to tune Ca2+ channel–vesicle.

Böhme, A., Beis, C., Reddy-Alla, S., Reynolds, E., Mampell, M. M., Grasskamp, A. T., et al. (2016). Active zone scaffolds differentially accumulate Unc13 isoforms to tune Ca2+ channel–vesicle. Nature Neuroscience, 19(10), 1311-1320. doi:10.1038/nn.4364.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-2236-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-6748-C
Genre: Journal Article

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 Creators:
Böhme, A., Author
Beis, C., Author
Reddy-Alla, S., Author
Reynolds, E., Author
Mampell, M. M., Author
Grasskamp, A. T., Author
Lützkendorf, J., Author
Dufour Bergeron, D. , Author
Driller, J. H., Author
Babikir, H., Author
Göttfert, F.1, Author              
Robinson, I. M., Author
O’Kane, C. J., Author
Hell, S. W.1, Author              
Wahl, M. C., Author
Stelzl, U., Author
Loll, B., Author
Walter, A. M., Author
Sigrist, S. J., Author
Affiliations:
1Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society, ou_578627              

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 Abstract: Brain function relies on fast and precisely timed synaptic vesicle (SV) release at active zones (AZs). Efficacy of SV release depends on distance from SV to Ca2+ channel, but molecular mechanisms controlling this are unknown. Here we found that distances can be defined by targeting two unc-13 (Unc13) isoforms to presynaptic AZ subdomains. Super-resolution and intravital imaging of developing Drosophila melanogaster glutamatergic synapses revealed that the Unc13B isoform was recruited to nascent AZs by the scaffolding proteins Syd-1 and Liprin-α, and Unc13A was positioned by Bruchpilot and Rim-binding protein complexes at maturing AZs. Unc13B localized 120 nm away from Ca2+ channels, whereas Unc13A localized only 70 nm away and was responsible for docking SVs at this distance. Unc13Anull mutants suffered from inefficient, delayed and EGTA-supersensitive release. Mathematical modeling suggested that synapses normally operate via two independent release pathways differentially positioned by either isoform. We identified isoform-specific Unc13-AZ scaffold interactions regulating SV-Ca2+-channel topology whose developmental tightening optimizes synaptic transmission.

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Language(s): eng - English
 Dates: 2016-08-152016-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nn.4364
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Title: Nature Neuroscience
Source Genre: Journal
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Pages: - Volume / Issue: 19 (10) Sequence Number: - Start / End Page: 1311 - 1320 Identifier: -