NDLI: PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

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PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

Content Provider	Scilit
Author	Kane, Lesley A. Lazarou, Michael Fogel, Adam I. Li, Yan Yamano, Koji Sarraf, Shireen Banerjee, Soojay Youle, Richard J.
Copyright Year	2014
Description	PINK1 kinase activates the E3 ubiquitin ligase Parkin to induce selective autophagy of damaged mitochondria. However, it has been unclear how PINK1 activates and recruits Parkin to mitochondria. Although PINK1 phosphorylates Parkin, other PINK1 substrates appear to activate Parkin, as the mutation of all serine and threonine residues conserved between Drosophila and human, including Parkin S65, did not wholly impair Parkin translocation to mitochondria. Using mass spectrometry, we discovered that endogenous PINK1 phosphorylated ubiquitin at serine 65, homologous to the site phosphorylated by PINK1 in Parkin’s ubiquitin-like domain. Recombinant TcPINK1 directly phosphorylated ubiquitin and phospho-ubiquitin activated Parkin E3 ubiquitin ligase activity in cell-free assays. In cells, the phosphomimetic ubiquitin mutant S65D bound and activated Parkin. Furthermore, expression of ubiquitin S65A, a mutant that cannot be phosphorylated by PINK1, inhibited Parkin translocation to damaged mitochondria. These results explain a feed-forward mechanism of PINK1-mediated initiation of Parkin E3 ligase activity.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003245/pdf
Ending Page	153
Page Count	11
Starting Page	143
DOI	10.1083/jcb.201402104
Journal	Journal of Cell Biology
Issue Number	2
Volume Number	205
Language	English
Publisher	Rockefeller University Press
Publisher Date	2014-04-28
Access Restriction	Open
Subject Keyword	Cell Biology Mitochondria E3 Ubiquitin Ligase Phosphorylated Activated Parkin Ubiquitin Activated Ubiquitin To Activate Parkin Journal: Journal of Cell Biology (Vol- 205, Issue- 2)
Content Type	Text

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