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Fig. 9 | Acta Neuropathologica Communications

Fig. 9

From: Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates

Fig. 9

A model of Ser129-phosphorylation role in regulating α-syn levels and forming α-syn aggregates. Mitochondrial impairment stimulates solubility change of α-syn proteins from normally soluble forms to insoluble forms. Also, mitochondrial impairment facilitates Ser129-phosphorylation of α-syn by an increase in influx of extracellular Ca2+. Ser129-phosphorylated α-syn, including soluble and insoluble forms, is targeted to the proteasome pathway. Proteasomal targeting of Ser129-phosphorylated α-syn is more promoted under lysosome inhibition. It acts as a suppressor complementary to the lysosome pathway against accumulation of insoluble α-syn proteins. Also, α-syn aggregates undergo Ser129-phosphorylation. However, Ser129-phosphorylation-mediated proteasomal targeting is ineffective, once α-syn aggregates turn to be degradation-resistant. Consequently, α-syn proteins deposited in aggregates are extensively phosphorylated

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