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...
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 |
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Format: | Article |
Language: | English |
Published: |
The Royal Society
2014-01-01
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Series: | Open Biology |
Subjects: | |
Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.130213 |
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