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- W2792899724 abstract "Human alpha-synuclein (aS), a protein relevant in the brain with so-far unknown function, plays an important role in Parkinson's disease. The phosphorylation state of aS was related to the disease, prompting interest in this process. The presumed physiological function and the disease action of aS involves membrane interaction. Here, we study the effect of phosphorylation at positions 87 and 129, mimicked by the mutations S87A, S129A (non-phosphorylated) and S87D, S129D (phosphorylated) on membrane binding [1]. Local binding is detected by spin-label continuous-wave electron paramagnetic resonance, by monitoring the mobility of the spin label. Low mobility shows membrane binding, high mobility local unbinding. For S87A/D, six positions (27, 56, 63, 69, 76, and 90) were spin labelled individually and probed by EPR; and for S129A/D, three (27, 56, and 69). Binding to large unilamellar vesicles of 100 nm diameter of 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1’-racglycerol) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine in a 1 : 1 composition is not affected by the phosphorylation state of S129. For phosphorylation at S87, local unbinding of aS from the membrane is observed. We speculate that modulating the local membrane affinity by phosphorylation could tune the way aS interacts with different membranes; for example, tuning its membrane-fusion activity. [1]Kumar et al. Isr. J. Chem. (2016) DOI: 10.1002/ijch.201600083" @default.
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- W2792899724 date "2018-02-01" @default.
- W2792899724 modified "2023-10-01" @default.
- W2792899724 title "Membrane Binding of Parkinson's Protein Alpha-Synuclein: Effect of Phosphorylation at Positions 87 and 129 by the S to D Mutation Approach" @default.
- W2792899724 doi "https://doi.org/10.1016/j.bpj.2017.11.2297" @default.
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