Arachidonic acid potentiates exocytosis and allows neuronal SNARE complex to interact with Munc18a

Latham, C. F., Osborne, S. L., Cryle, M. J. and Meunier, F. A. (2007) Arachidonic acid potentiates exocytosis and allows neuronal SNARE complex to interact with Munc18a. Journal of Neurochemistry, 100 6: 1543-1554. doi:10.1111/j.1471-4159.2006.04286.x

Author Latham, C. F.
Osborne, S. L.
Cryle, M. J.
Meunier, F. A.
Title Arachidonic acid potentiates exocytosis and allows neuronal SNARE complex to interact with Munc18a
Journal name Journal of Neurochemistry   Check publisher's open access policy
ISSN 0022-3042
Publication date 2007-03
Year available 2006
Sub-type Article (original research)
DOI 10.1111/j.1471-4159.2006.04286.x
Volume 100
Issue 6
Start page 1543
End page 1554
Total pages 12
Place of publication Oxford
Publisher Blackwell Publishing
Collection year 2008
Language eng
Subject 270107 Cell Neurochemistry
780105 Biological sciences
Abstract Neuronal communication relies on the fusion of neurotransmitter-containing vesicles with the neuronal plasma membrane. Recent genetic studies have highlighted the critical role played by polyunsaturated fatty acids in neurotransmission, however, there is little information available about which fatty acids act on exocytosis and, more importantly, by what mechanism. We have used permeabilized chromaffin cells to screen various fatty acids of the n-3 and n-6 series for their acute effects on exocytosis. We have demonstrated that an n-6 series polyunsaturated fatty acid, arachidonic acid, potentiates secretion from intact neurosecretory cells regardless of the secretagogue used. We have shown that arachidonic acid dose dependently increases soluble NSF attachment protein receptor complex formation in chromaffin cells and bovine cortical brain extracts and that a non-hydrolysable analogue of arachidonic acid causes a similar increase in SNARE complex formation. This prompted us to examine the effect of arachidonic acid on SNARE protein interactions with Munc18a, a protein known to prevent Syntaxin1a engagement into the SNARE complex in vitro. In the presence of arachidonic acid, we show that Munc18a can interact with the neuronal SNARE complex in a dose-dependent manner. We further demonstrate that arachidonic acid directly interacts with Syntaxin1a.
Keyword Biochemistry & Molecular Biology
arachidonic acid
soluble NSF attachment protein receptor
Adrenal Chromaffin Cells
Synaptic Vesicle Docking
Botulinum Toxin
Catecholamine Secretion
Triggered Exocytosis
Protein Interactions
Phospholipase A(2)
Structural Basis
Q-Index Code C1
Q-Index Status Confirmed Code

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Created: Mon, 18 Feb 2008, 16:30:37 EST