Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity

Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity

Mutations in PINK1 and Parkin are associated with early-onset Parkinson's disease. We recently discovered that PINK1 phosphorylates Parkin at serine65 (Ser65) within its Ubl domain, leading to its activation in a substrate-free activity assay. We now demonstrate the critical requirement of Ser6...

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Bibliographic Details
Main Authors: Agne Kazlauskaite, Van Kelly, Clare Johnson, Carla Baillie, C. James Hastie, Mark Peggie, Thomas Macartney, Helen I. Woodroof, Dario R. Alessi, Patrick G. A. Pedrioli, Miratul M. K. Muqit
Format: Article
Language:English
Published: The Royal Society 2014-01-01
Series:Open Biology
Subjects:
parkin
pink1
miro1
ubiquitin
phosphorylation
parkinson's disease
Online Access:https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.130213

Internet

https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.130213

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