Ham S, Yun SP, Kim H, Kim D, Seo BA, Kim H, Shin JY, Dar MA, Lee GH, Lee YI, Kim D, Kim S, Kweon HS, Shin JH, Ko HS, Lee Y. Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion. Sci Transl Med. 2020 Nov 11;12(569) PubMed.

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  1. While mutations in parkin are associated with early onset parkinsonism, this has generally been thought to be pathologically distinct from idiopathic Parkinson's disease. Most parkin patients who have come to autopsy do not have the α-synuclein Lewy bodies which are diagnostic of Parkinson's disease.

    Previous work has demonstrated that parkin knockout in mice does not lead to α-synuclein aggregation either, consistent with human neuropathology. However, these mice do have elevated AIMP2, and previous work has suggested that reduced parkin leads to elevated AIMP2, and increased cell death through parthanatos.

    The current paper suggests that, in addition to this putatively α-synuclein-independent mode of cell death leading to parkinsonism, AIMP2 can cause or exacerbate α-synuclein aggregation and may be involved in idiopathic PD. This intriguing finding brings together two distinct fields and could have implications for our understanding of disease pathogenesis.

    View all comments by Michael Henderson

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