Quantitative super-resolution imaging of Bruchpilot distinguishes active zone states

Nadine Ehmann, Sebastian van de Linde, Amit Alon, Dmitrij Ljaschenko, Xi Zhen Keung, Thorge Holm, Annika Rings, Aaron DiAntonio, Stefan Hallermann, Uri Ashery, Manfred Heckmann, Markus Sauer () and Robert J. Kittel ()
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Nadine Ehmann: Institute of Physiology, University of Würzburg
Sebastian van de Linde: University of Würzburg
Amit Alon: Wise Faculty of Life Sciences, Tel Aviv University
Dmitrij Ljaschenko: Institute of Physiology, University of Würzburg
Xi Zhen Keung: Institute of Physiology, University of Würzburg
Thorge Holm: University of Würzburg
Annika Rings: European Neuroscience Institute, University Medical Center Göttingen
Aaron DiAntonio: Washington University School of Medicine
Stefan Hallermann: European Neuroscience Institute, University Medical Center Göttingen
Uri Ashery: Wise Faculty of Life Sciences, Tel Aviv University
Manfred Heckmann: Institute of Physiology, University of Würzburg
Markus Sauer: University of Würzburg
Robert J. Kittel: Institute of Physiology, University of Würzburg

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract The precise molecular architecture of synaptic active zones (AZs) gives rise to different structural and functional AZ states that fundamentally shape chemical neurotransmission. However, elucidating the nanoscopic protein arrangement at AZs is impeded by the diffraction-limited resolution of conventional light microscopy. Here we introduce new approaches to quantify endogenous protein organization at single-molecule resolution in situ with super-resolution imaging by direct stochastic optical reconstruction microscopy (dSTORM). Focusing on the Drosophila neuromuscular junction (NMJ), we find that the AZ cytomatrix (CAZ) is composed of units containing ~137 Bruchpilot (Brp) proteins, three quarters of which are organized into about 15 heptameric clusters. We test for a quantitative relationship between CAZ ultrastructure and neurotransmitter release properties by engaging Drosophila mutants and electrophysiology. Our results indicate that the precise nanoscopic organization of Brp distinguishes different physiological AZ states and link functional diversification to a heretofore unrecognized neuronal gradient of the CAZ ultrastructure.

Date: 2014
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DOI: 10.1038/ncomms5650

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