Vivid views of the PINK1 protein

Daou, Salima; Sicheri, Frank

doi:10.1038/d41586-017-07691-x

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06 December 2017

Vivid views of the PINK1 protein

Structures of an unusual enzymatic domain in PINK1 provide insights into how this protein regulates the function of organelles called mitochondria, and how mutations in PINK1 contribute to Parkinson’s disease.

Salima Daou⁰ &
Frank Sicheri¹

Salima Daou
1. Salima Daou is at the Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario M5G 1X5, Canada.
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Frank Sicheri
1. Frank Sicheri is at the Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario M5G 1X5, Canada, and in the Departments of Molecular Genetics and of Biochemistry, University of Toronto.
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When essential cellular organelles called mitochondria that act as the cell’s energy factories are damaged, the cell’s response is coordinated by two proteins — PINK1 and parkin¹. Mutations in the genes that encode these proteins are among the most prevalent in hereditary early-onset Parkinson’s disease². Our understanding of how parkin functions and how mutations in parkin contribute to Parkinson’s disease has benefited immensely from atomic-resolution snapshots of the protein in action³^–⁵. But owing to difficulties in atomic-level imaging of PINK1, our understanding of its equally important role in these processes has been hindered. Two studies (one on page 51 by Schubert et al.⁶, and one in eLife by Kumar et al.⁷) have overcome these hurdles to provide near atomic-scale views of PINK1, providing invaluable insight into its mechanism of action.

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Nature 552, 38-39 (2017)

doi: https://doi.org/10.1038/d41586-017-07691-x

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