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

Bademosi, Adekunle T., Lauwers, Elsa, Padmanabhan, Pranesh, Odierna, Lorenzo, Chai, Ye Jin, Papadopulos, Andreas, Goodhill, Geoffrey J., Verstreken, Patrik, Van Swinderen, Bruno and Meunier, Frederic A. (2017) In vivo single-molecule imaging of syntaxin1A reveals polyphosphoinositide- and activity-dependent trapping in presynaptic nanoclusters. Nature Communications, 8 . doi:10.1038/ncomms13660


Author Bademosi, Adekunle T.
Lauwers, Elsa
Padmanabhan, Pranesh
Odierna, Lorenzo
Chai, Ye Jin
Papadopulos, Andreas
Goodhill, Geoffrey J.
Verstreken, Patrik
Van Swinderen, Bruno
Meunier, Frederic A.
Title In vivo single-molecule imaging of syntaxin1A reveals polyphosphoinositide- and activity-dependent trapping in presynaptic nanoclusters
Formatted title
In vivo single-molecule imaging of syntaxin1A reveals polyphosphoinositide- and activity-dependent trapping in presynaptic nanoclusters
Journal name Nature Communications   Check publisher's open access policy
ISSN 2041-1723
Publication date 2017-01-03
Sub-type Article (original research)
DOI 10.1038/ncomms13660
Open Access Status DOI
Volume 8
Total pages 15
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Collection year 2018
Language eng
Formatted 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Mathematics and Physics
HERDC Pre-Audit
Queensland Brain Institute Publications
School of Biomedical Sciences Publications
 
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