In vivo single-molecule imaging of syntaxin1A reveals polyphosphoinositide- and activity-dependent trapping in presynaptic nanoclusters

Adekunle T. Bademosi, Elsa Lauwers, Pranesh Padmanabhan, Lorenzo Odierna, Ye Jin Chai, Andreas Papadopulos, Geoffrey J. Goodhill, Patrik Verstreken, Bruno van Swinderen and Frédéric A. Meunier ()
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Adekunle T. Bademosi: Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Elsa Lauwers: VIB Center for the Biology of Disease
Pranesh Padmanabhan: Queensland Brain Institute, The University of Queensland
Lorenzo Odierna: School of Biomedical Sciences, The University of Queensland
Ye Jin Chai: Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Andreas Papadopulos: Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Geoffrey J. Goodhill: Queensland Brain Institute, The University of Queensland
Patrik Verstreken: VIB Center for the Biology of Disease
Bruno van Swinderen: Queensland Brain Institute, The University of Queensland
Frédéric A. Meunier: Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland

Nature Communications, 2016, vol. 7, issue 1, 1-17

Abstract: Abstract Syntaxin1A is organized in nanoclusters that are critical for the docking and priming of secretory vesicles from neurosecretory cells. Whether and how these nanoclusters are affected by neurotransmitter release in nerve terminals from a living organism is unknown. Here we imaged photoconvertible syntaxin1A-mEos2 in the motor nerve terminal of Drosophila larvae by single-particle tracking photoactivation localization microscopy. Opto- and thermo-genetic neuronal stimulation increased syntaxin1A-mEos2 mobility, and reduced the size and molecular density of nanoclusters, suggesting an activity-dependent release of syntaxin1A from the confinement of nanoclusters. Syntaxin1A mobility was increased by mutating its polyphosphoinositide-binding site or preventing SNARE complex assembly via co-expression of tetanus toxin light chain. In contrast, syntaxin1A mobility was reduced by preventing SNARE complex disassembly. Our data demonstrate that polyphosphoinositide favours syntaxin1A trapping, and show that SNARE complex disassembly leads to syntaxin1A dissociation from nanoclusters. Lateral diffusion and trapping of syntaxin1A in nanoclusters therefore dynamically regulate neurotransmitter release.

Date: 2016
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DOI: 10.1038/ncomms13660

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