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α-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis
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α-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis
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Journal Article
α-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis
2010
Overview
α‐Synuclein is a synaptic modulatory protein implicated in the pathogenesis of Parkinson disease. The precise functions of this small cytosolic protein are still under investigation. α‐Synuclein has been proposed to regulate soluble
N
‐ethylmaleimide‐sensitive factor attachment protein receptor (SNARE) proteins involved in vesicle fusion. Interestingly, α‐synuclein fails to interact with SNARE proteins in conventional protein‐binding assays, thus suggesting an indirect mode of action. As the structural and functional properties of both α‐synuclein and the SNARE proteins can be modified by arachidonic acid, a common lipid regulator, we analysed this possible tripartite link in detail. Here, we show that the ability of arachidonic acid to stimulate SNARE complex formation and exocytosis can be controlled by α‐synuclein, both
in vitro
and
in vivo
. α‐Synuclein sequesters arachidonic acid and thereby blocks the activation of SNAREs. Our data provide mechanistic insights into the action of α‐synuclein in the modulation of neurotransmission.
The fatty acid‐binding protein alpha‐synuclein has been proposed to regulate SNARE proteins. This report shows that alpha‐synuclein sequesters fatty acids to down‐regulate SNARE assembly thereby inhibiting exocytosis.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Nature Publishing Group
Subject
/ alpha-Synuclein - metabolism
/ Animals
/ Arachidonic Acid - metabolism
/ Chromaffin Cells - metabolism
/ EMBO20
/ EMBO27
/ Humans
/ Mice
/ Rats
/ SNARE
/ Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - genetics
/ Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - metabolism
/ Synaptosomal-Associated Protein 25 - genetics
/ Synaptosomal-Associated Protein 25 - metabolism
/ syntaxin
