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Journal Article

Controlling synaptotagmin activity by electrostatic screening.

MPS-Authors
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Hernandez,  J. M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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van den Bogaart,  G.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Ahmed,  S.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Holt,  M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Fulltext (public)

1539321.pdf
(Publisher version), 989KB

Supplementary Material (public)

1539321-Suppl.pdf
(Supplementary material), 609KB

Citation

Park, Y., Hernandez, J. M., van den Bogaart, G., Ahmed, S., Holt, M., Riedel, D., et al. (2012). Controlling synaptotagmin activity by electrostatic screening. Nature Structural and Molecular Biology, 19(10), 991-997. doi:10.1038/nsmb.2375.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-EBFE-9
Abstract
Exocytosis of neurosecretory vesicles is mediated by the SNARE (soluble N-ethylmaleimide–sensitive factor attachment protein receptor) proteins syntaxin-1, synaptobrevin and SNAP-25, with synaptotagmin functioning as the major Ca2+ sensor for triggering membrane fusion. Here we show that bovine chromaffin granules readily fuse with large unilamellar liposomes in a SNARE-dependent manner. Fusion is enhanced by Ca2+, but only when the target liposomes contain phosphatidylinositol-4,5-bisphosphate and when polyphosphate anions, such as nucleotides or pyrophosphate, are present. Ca2+-dependent enhancement is mediated by endogenous synaptotagmin-1. Polyphosphates operate by an electrostatic mechanism that reverses an inactivating cis association of synaptotagmin-1 with its own membrane without affecting trans binding. Hence, the balancing of trans- and cis-membrane interactions of synaptotagmin-1 could be a crucial element in the pathway of Ca2+-dependent exocytosis.