Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion
Sangwoo Ham, Seung Pil Yun, Hyojung Kim, Donghoon Kim, Bo Am Seo, Heejeong Kim, Jeong‐Yong Shin, Mohammad Aasif Dar, Gum Hwa Lee, Yun Il Lee, Yun Il Lee, Doyeun Kim, Sung‐Hoon Kim, Hee-Seok Kweon, Joo‐Ho Shin, Han Seok Ko, Yunjong Lee, Yunjong Lee
Abstract
deletion, or oxidative stress triggered a redistribution of both AIMP2 and α-synuclein into insoluble fraction in cells and in vivo. Supporting the pathogenic role of AIMP2, AIMP2 knockdown ameliorated the α-synuclein aggregation and dopaminergic cell death in response to PFF or 6-hydroxydopamine treatment. Together, our results suggest that AIMP2 plays a pathological role in the aggregation of α-synuclein in mice. Because AIMP2 insolubility and coaggregation with α-synuclein have been seen in the PD Lewy body, targeting pathologic AIMP2 aggregation might be useful as a therapeutic strategy for neurodegenerative α-synucleinopathies.