Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Biochemistry. 2013 Apr 9;52(14):2385-7. doi: 10.1021/bi4002369. Epub 2013 Mar 27.
The native function of α-synuclein is thought to involve regulation of synaptic vesicle trafficking. Recent work has also implicated a role in neurotransmission, possibly through interactions with the proteins involved in synaptic vesicle fusion. Here, we demonstrate that α-synuclein inhibits SNARE-mediated vesicle fusion through binding the membrane, without a direct interaction between α-synuclein and any of the SNARE proteins. This work supports a model in which α-synuclein plays a role in the regulation of vesicle fusion by modulating properties of the lipid bilayer.
α-突触核蛋白的天然功能被认为涉及调节突触囊泡运输。最近的工作还表明它在神经递质传递中起作用,可能是通过与参与突触囊泡融合的蛋白质相互作用。在这里,我们证明 α-突触核蛋白通过结合膜来抑制 SNARE 介导的囊泡融合,而无需 α-突触核蛋白与任何 SNARE 蛋白之间的直接相互作用。这项工作支持了这样一种模型,即 α-突触核蛋白通过调节脂质双层的性质在调节囊泡融合中发挥作用。