Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation

Masahiro Iguchi, Yuki Kujuro, Kei Okatsu, Fumika Koyano, Hidetaka Kosako, Mayumi Kimura, Norihiro Suzuki, Shinichiro Uchiyama, Keiji Tanaka, Noriyuki Matsuda

Research output: Contribution to journalArticlepeer-review

162 Citations (Scopus)


Background: Parkin is a ubiquitin ligase activated by a decrease in the mitochondrial membrane potential (Δ Φm). However, details regarding its mechanism remain limited. Results: PINK1-dependent phosphorylation of Parkin at Ser-65 following dissipation of Δ Φm triggers ubiquitin-ester transfer by the RING2 domain of Parkin to Cys-431. Conclusion: Parkin catalyzes trans- (ubiquitin-thioester)ification upon PINK1-dependent phosphorylation. Significance: The molecular process of Parkin-catalyzed ubiquitylation has been determined.

Original languageEnglish
Pages (from-to)22019-22032
Number of pages14
JournalJournal of Biological Chemistry
Issue number30
Publication statusPublished - 2013 Jul 26
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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