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 journalArticle

121 Citations (Scopus)

Abstract

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
Volume288
Issue number30
DOIs
Publication statusPublished - 2013 Jul 26

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation'. Together they form a unique fingerprint.

  • Cite this

    Iguchi, M., Kujuro, Y., Okatsu, K., Koyano, F., Kosako, H., Kimura, M., Suzuki, N., Uchiyama, S., Tanaka, K., & Matsuda, N. (2013). Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation. Journal of Biological Chemistry, 288(30), 22019-22032. https://doi.org/10.1074/jbc.M113.467530