NEUROTOXICITY OF ALFA-SYNUCLEIN IN
PARKINSON’S DISEASE
Intracellular
protein aggregates called Lewy bodies are the characteristic pathological
lesions of Parkinson’s 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 Parkinson’s 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 Parkinson’s 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.