TY - JOUR
T1 - Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation
AU - Iguchi, Masahiro
AU - Kujuro, Yuki
AU - Okatsu, Kei
AU - Koyano, Fumika
AU - Kosako, Hidetaka
AU - Kimura, Mayumi
AU - Suzuki, Norihiro
AU - Uchiyama, Shinichiro
AU - Tanaka, Keiji
AU - Matsuda, Noriyuki
N1 - Funding Information:
This work was supported in part by Japan Society for the Promotion of Science (JSPS)/Ministry of Education, Culture, Sports, Science and Technology (MEXT) KAKENHI Grants 23-6061 (to K. O.), 23791001 (to Y. K.), 21000012 (to K. T.), and 23687018, 24111557, and 25112522 (to N. M.); the Tomizawa Jun-ichi and Keiko Fund for Young Scientist (to N. M.); and the Takeda Science Foundation (to H. K., N. M., and K. T.). Supported by Tomizawa Jun-ichi and Keiko Fund of Molecular Biology Society of Japan for Young Scientist. We thank Dr. J. Shen for providing PINK1-/- MEFs, Dr. M. Shindo for evaluation of MS data, and Dr. T. Kitamura for the PLAT-E cells. We also thank Drs. N. Tani and H. Taniguchi for help with the LC-MS/MS analysis. We thank Dr. J. Shen for providing PINK1 MEFs, Dr. M. Shindo for evaluation of MS data, and Dr. T. Kitamura for the PLAT-E cells. We also thank Drs. N. Tani and H. Taniguchi for help with the LC-MS/MS analysis.
PY - 2013/7/26
Y1 - 2013/7/26
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84881260124
UR - https://www.scopus.com/pages/publications/84881260124#tab=citedBy
U2 - 10.1074/jbc.M113.467530
DO - 10.1074/jbc.M113.467530
M3 - Article
C2 - 23754282
AN - SCOPUS:84881260124
SN - 0021-9258
VL - 288
SP - 22019
EP - 22032
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 30
ER -