IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v510y2014i7503d10.1038_nature13392.html
   My bibliography  Save this article

Ubiquitin is phosphorylated by PINK1 to activate parkin

Author

Listed:
  • Fumika Koyano

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan
    Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba 277-8561, Japan)

  • Kei Okatsu

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan
    Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba 277-8561, Japan)

  • Hidetaka Kosako

    (Fujii Memorial Institute of Medical Sciences, The University of Tokushima, Tokushima 770-8503, Japan)

  • Yasushi Tamura

    (Research Center for Materials Science, Nagoya University, Nagoya, Aichi 464-8602, Japan)

  • Etsu Go

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Mayumi Kimura

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Yoko Kimura

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan
    Graduate School of Agriculture, Shizuoka University, 836 Ohya, Shizuoka 422-8529, Japan)

  • Hikaru Tsuchiya

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Hidehito Yoshihara

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Takatsugu Hirokawa

    (Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan)

  • Toshiya Endo

    (Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
    JST-CREST/Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, Japan)

  • Edward A. Fon

    (McGill Parkinson Program, Montreal Neurological Institute and Hospital, McGill University, Montréal, Québec H3A 2B4, Canada)

  • Jean-François Trempe

    (McGill University, Montréal, Québec H3G 1Y6, Canada)

  • Yasushi Saeki

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Keiji Tanaka

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

  • Noriyuki Matsuda

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan
    Protein Metabolism Project, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan)

Abstract

Ubiquitin, known for its role in post-translational modification of other proteins, undergoes post-translational modification itself; after a decrease in mitochondrial membrane potential, the kinase enzyme PINK1 phosphorylates ubiquitin at Ser 65, and the phosphorylated ubiquitin then interacts with ubiquitin ligase (E3) enzyme parkin, which is also phosphorylated by PINK1, and this process is sufficient for full activation of parkin enzymatic activity.

Suggested Citation

  • Fumika Koyano & Kei Okatsu & Hidetaka Kosako & Yasushi Tamura & Etsu Go & Mayumi Kimura & Yoko Kimura & Hikaru Tsuchiya & Hidehito Yoshihara & Takatsugu Hirokawa & Toshiya Endo & Edward A. Fon & Jean-, 2014. "Ubiquitin is phosphorylated by PINK1 to activate parkin," Nature, Nature, vol. 510(7503), pages 162-166, June.
    • Handle: RePEc:nat:nature:v:510:y:2014:i:7503:d:10.1038_nature13392
    DOI: 10.1038/nature13392
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature13392
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature13392?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Xiangyi S. Wang & Thomas R. Cotton & Sarah J. Trevelyan & Lachlan W. Richardson & Wei Ting Lee & John Silke & Bernhard C. Lechtenberg, 2023. "The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Ryosuke Ishimura & Afnan H. El-Gowily & Daisuke Noshiro & Satoko Komatsu-Hirota & Yasuko Ono & Mayumi Shindo & Tomohisa Hatta & Manabu Abe & Takefumi Uemura & Hyeon-Cheol Lee-Okada & Tarek M. Mohamed , 2022. "The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Véronique Sauvé & Eric Stefan & Nathalie Croteau & Thomas Goiran & Rayan Fakih & Nupur Bansal & Adelajda Hadzipasic & Jing Fang & Paramasivam Murugan & Shimin Chen & Edward A. Fon & Warren D. Hirst & , 2024. "Activation of parkin by a molecular glue," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    4. Katrin Stuber & Tobias Schneider & Jill Werner & Michael Kovermann & Andreas Marx & Martin Scheffner, 2021. "Structural and functional consequences of NEDD8 phosphorylation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    5. Trendelina Rrustemi & Katrina Meyer & Yvette Roske & Bora Uyar & Altuna Akalin & Koshi Imami & Yasushi Ishihama & Oliver Daumke & Matthias Selbach, 2024. "Pathogenic mutations of human phosphorylation sites affect protein–protein interactions," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    6. Huan Yang & Caroline Sibilla & Raymond Liu & Jina Yun & Bruce A. Hay & Craig Blackstone & David C. Chan & Robert J. Harvey & Ming Guo, 2022. "Clueless/CLUH regulates mitochondrial fission by promoting recruitment of Drp1 to mitochondria," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    7. Hayden Weng Siong Tan & Guang Lu & Han Dong & Yik-Lam Cho & Auginia Natalia & Liming Wang & Charlene Chan & Dennis Kappei & Reshma Taneja & Shuo-Chien Ling & Huilin Shao & Shih-Yin Tsai & Wen-Xing Din, 2022. "A degradative to secretory autophagy switch mediates mitochondria clearance in the absence of the mATG8-conjugation machinery," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    8. Lene Clausen & Vasileios Voutsinos & Matteo Cagiada & Kristoffer E. Johansson & Martin Grønbæk-Thygesen & Snehal Nariya & Rachel L. Powell & Magnus K. N. Have & Vibe H. Oestergaard & Amelie Stein & Do, 2024. "A mutational atlas for Parkin proteostasis," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    9. Qiang Zhu & Matthew E. Combs & Juan Liu & Xue Bai & Wenbo B. Wang & Laura E. Herring & Jiandong Liu & Jason W. Locasale & Dawn E. Bowles & Ryan T. Gross & Michelle Mendiola Pla & Christopher P. Mack &, 2023. "GRAF1 integrates PINK1-Parkin signaling and actin dynamics to mediate cardiac mitochondrial homeostasis," Nature Communications, Nature, vol. 14(1), pages 1-21, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:510:y:2014:i:7503:d:10.1038_nature13392. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.