Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers.

ABSTRACT:

Background

In several neurodegenerative diseases, hyperphosphorylation at position Ser129 is found in fibrillar deposits of alpha-synuclein (asyn), implying a pathophysiological role of asyn phosphorylation in neurodegeneration. However, recent animal models applying asyn phosphorylation mimics demonstrated a protective effect of phosphorylation. Since metal-ion induced asyn oligomers were identified as a potential neurotoxic aggregate species with membrane pore-forming abilities, the current study was undertaken to determine effects of asyn phosphorylation on oligomer membrane binding.

Methods

We investigated the influence of S129 phosphorylation on interactions of metal-ion induced asyn oligomers with small unilamellar lipid vesicles (SUV) composed of POPC and DPPC applyin

SUBMITTER: Nubling GS 

PROVIDER: S-EPMC4049638 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature