首页    期刊浏览 2024年12月13日 星期五
登录注册

文章基本信息

  • 标题:The number of α-synuclein proteins per vesicle gives insights into its physiological function
  • 本地全文:下载
  • 作者:Mohammad A. A. Fakhree ; Niels Zijlstra ; Christian C. Raiss
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2016
  • 卷号:6
  • 期号:1
  • DOI:10.1038/srep30658
  • 语种:English
  • 出版社:Springer Nature
  • 摘要:Although it is well established that the protein α-synuclein (αS) plays an important role in Parkinson's disease, its physiological function remains largely unknown. It has been reported to bind membranes and to play a role in membrane remodeling processes. The mechanism by which αS remodels membranes is still debated; it may either affect its physical properties or act as a chaperone for other membrane associated proteins. To obtain insight into the role of αS in membrane remodeling we investigated the number of αS proteins associated with single small vesicles in a neuronal cell model. Using single-molecule microscopy and photo-bleaching approaches, we most frequently found 70 αS-GFPs per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of αS, per vesicle. We therefore hypothesize a dual, synergistic role for αS in membrane remodeling.
国家哲学社会科学文献中心版权所有