Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.

@article{Stckl2008AlphasynucleinSB,
  title={Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.},
  author={Martin St{\"o}ckl and Patricia Fischer and Erich E. Wanker and Andreas Herrmann},
  journal={Journal of molecular biology},
  year={2008},
  volume={375 5},
  pages={1394-404}
}
Previous studies indicate that binding of alpha-synuclein to membranes is critical for its physiological function and the development of Parkinson's disease (PD). Here, we have investigated the association of fluorescence-labeled alpha-synuclein variants with different types of giant unilamellar vesicles using confocal microscopy. We found that alpha-synuclein binds with high affinity to anionic phospholipids, when they are embedded in a liquid-disordered as opposed to a liquid-ordered… CONTINUE READING
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