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The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding

Lazarou, Michael, Narendra, Derek P., Jin, Seok Min, Tekle, Ephrem, Banerjee, Soojay, Youle, Richard J.·2013·Journal of Cell Biology
DOI 10.1083/jcb.201210111PMC PMC3549971
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Abstract

Genetic studies indicate that the mitochondrial kinase PINK1 and the RING-between-RING E3 ubiquitin ligase Parkin function in the same pathway. In concurrence, mechanistic studies show that PINK1 can recruit Parkin from the cytosol to the mitochondria, increase the ubiquitination activity of Parkin, and induce Parkin-mediated mitophagy. Here, we used a cell-free assay to recapitulate PINK1-dependent activation of Parkin ubiquitination of a validated mitochondrial substrate, mitofusin 1. We show that PINK1 activated the formation of a Parkin–ubiquitin thioester intermediate, a hallmark of HECT E3 ligases, both in vitro and in vivo. Parkin HECT-like ubiquitin ligase activity was essential for PINK1-mediated Parkin translocation to mitochondria and mitophagy. Using an inactive Parkin mutant, we found that PINK1 stimulated Parkin self-association and complex formation upstream of mitochondrial translocation. Self-association occurred independent of ubiquitination activity through the RING-between-RING domain, providing mechanistic insight into how PINK1 activates Parkin.

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Crossref · 10.1083/jcb.201210111

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  • USP8 has little effect on the ubiquitination or stability of other known mitochondrial substrates of parkin.

    “Moreover, we find that USP8 preferentially removes K6-linked Ub conjugates from parkin but has little effect on the ubiquitination or stability of other known mitochondrial substrates of parkin.”

    From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Lazarou et al, 2013

    The Results and discussion identify mitochondrial Parkin substrates, including Mfn1 and MitoNEET, and examine their ubiquitination. Searches for USP8 and its effects on substrate ubiquitination or stability found no passage addressing that claim in our copy. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

  • CCCP treatment induces a transient upward shift in parkin electrophoretic mobility, consistent with parkin activation and auto-ubiquitination.

    “Concurrently with the changes in parkin levels, the electrophoretic mobility of parkin was transiently shifted upward, consistent with a CCCP-induced activation of parkin and parkin auto-ubiquitination, as reported previously (Matsuda et al, 2010;Lazarou et al, 2013).”

    From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Lazarou et al, 2013

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Citations

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Research works printed but not linked: 29

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Metadata

Authors
Lazarou, M., Narendra, D. P., Jin, S. M., Tekle, E., Banerjee, S., & Youle, R. J.
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2013-01-14
Volume
200
Issue
2
Pages
163-172
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201210111
PMC
PMC3549971
Cited by
236
References
11
Language
en

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