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. 2014 Jun 9;9(6):e98906. doi: 10.1371/journal.pone.0098906

Figure 4. Schematic illustrating the influence of mimicking Ser129 phosphorylation on asyn membrane interactions.

Figure 4

A. For stressed gel-state membranes (DPPC-SUV), mimicking phosphorylation at Ser129 mildly reduces asyn binding affinity. B. Both pseudophosphorylated and unphosphorylated asyn monomers show no affinity to membranes in the liquid-crystalline state (POPC). C. Fe3+ induced asyn oligomers show a high membrane affinity and potentially act as membrane pores. Pseudophosphorylation at Ser129 shows a differential influence on asyn aggregation and binding behaviour. While increasing oligomer formation in presence of trivalent metal-ions, Ser129 pseudophosphorylation inhibits membrane binding and may thus allow oligomer sequestration into larger aggregates such as fibrils.

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