![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Article |
|---|---|
| Title: | Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains |
| Creators Name: | Stoeckl, M., Fischer, P., Wanker, E.E. and Herrmann, A. |
| Abstract: | 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 environment. This indicates that not only electrostatic forces but also lipid packing and hydrophobic interactions are critical for the association of alpha-synuclein with membranes in vitro. When compared to wild-type alpha-synuclein, the disease-causing alpha-synuclein variant A30P bound less efficiently to anionic phospholipids, while the variant E46K showed enhanced binding. This suggests that the natural association of alpha-synuclein with membranes is altered in the inherited forms of Parkinson's disease. |
| Keywords: | Lipid Domains, Greek Small Letter Alpha-Synuclein, Mutants, Giant Unilamellar Vesicles, Fluorescence Microscopy |
| Source: | Journal of Molecular Biology |
| ISSN: | 0022-2836 |
| Publisher: | Elsevier |
| Volume: | 375 |
| Number: | 5 |
| Page Range: | 1394-1404 |
| Date: | 1 February 2008 |
| Official Publication: | https://doi.org/10.1016/j.jmb.2007.11.051 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
