NEUROTOXICITY OF ALFA-SYNUCLEIN IN PARKINSONíS DISEASE††
Intracellular protein aggregates called Lewy bodies are the characteristic pathological lesions of Parkinsonís disease. In these inclusion bodies, alfa-synuclein is phosphorylated at serine 129 (Ser 129). Li Chen and Mel Feany (α-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinsonís disease. Nature Neuroscience 8, 657-663, 2005) define the role of phosphorylation of Ser 129 in alfa-synuclein toxicity and inclusion formation using a Drosophila model of Parkinsonís disease.
Ser 129 phosphorylation is crucial in alfa-synuclein toxicity and inclusion formation. Since blocking phosphorylation reduces toxicity and increases aggregate formation, authors conclude for a protective role of inclusions in alfa-synuclein toxicity.