Please use this identifier to cite or link to this item:
Título : α-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis
Autor : Darios, Frédéric, Ruipérez, Violeta, López-Font, Inmaculada, Villanueva, José, Gutiérrez, Luis M., Davletov, Bazbek
Fecha de publicación : Jul-2010
Editor: Nature Publishing Group
Resumen: 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.
Descripción : 6 p., 4 figures and references.
Versión del editor:
ISSN: 1469-221X
DOI: 10.1038/embor.2010.66
Citación : EMBO Reports 11(7): 528-533 (2010)
Appears in Collections:(IN) Artículos

Files in This Item:
File Description SizeFormat 
restringido.pdf21,67 kBAdobe PDFView/Open
Show full item record

Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.