IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v522y2015i7556d10.1038_nature14506.html
   My bibliography  Save this article

Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus

Author

Listed:
  • Keisuke Mochida

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology)

  • Yu Oikawa

    (Frontier Research Center, Tokyo Institute of Technology)

  • Yayoi Kimura

    (Advanced Medical Research Center, Yokohama City University)

  • Hiromi Kirisako

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
    CREST, Japan Science and Technology Agency)

  • Hisashi Hirano

    (Advanced Medical Research Center, Yokohama City University)

  • Yoshinori Ohsumi

    (Frontier Research Center, Tokyo Institute of Technology)

  • Hitoshi Nakatogawa

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
    CREST, Japan Science and Technology Agency)

Abstract

In yeast, the novel protein Atg40 is enriched in the cortical and cytoplasmic endoplasmic reticulum (ER), and loads these ER subdomains into autophagosomes to facilitate ER autophagy; Atg39 localizes to the perinuclear ER and induces autophagic sequestration of part of the nucleus, thus ensuring cell survival under nitrogen-deprived conditions.

Suggested Citation

  • Keisuke Mochida & Yu Oikawa & Yayoi Kimura & Hiromi Kirisako & Hisashi Hirano & Yoshinori Ohsumi & Hitoshi Nakatogawa, 2015. "Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus," Nature, Nature, vol. 522(7556), pages 359-362, June.
  • Handle: RePEc:nat:nature:v:522:y:2015:i:7556:d:10.1038_nature14506
    DOI: 10.1038/nature14506
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14506
    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/nature14506?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. Taeko Sasaki & Yasuharu Kushida & Takuya Norizuki & Hidetaka Kosako & Ken Sato & Miyuki Sato, 2024. "ALLO-1- and IKKE-1-dependent positive feedback mechanism promotes the initiation of paternal mitochondrial autophagy," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Ning Wang & Yoko Shibata & Joao A. Paulo & Steven P. Gygi & Tom A. Rapoport, 2023. "A conserved membrane curvature-generating protein is crucial for autophagosome formation in fission yeast," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Shuangcheng Alivia Wu & Chenchen Shen & Xiaoqiong Wei & Xiawei Zhang & Siwen Wang & Xinxin Chen & Mauricio Torres & You Lu & Liangguang Leo Lin & Huilun Helen Wang & Allen H. Hunter & Deyu Fang & Shen, 2023. "The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    4. Yun Xiang & Rui Lyu & Junjie Hu, 2023. "Oligomeric scaffolding for curvature generation by ER tubule-forming proteins," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    5. Patricia González-Rodríguez & Daniel J. Klionsky & Bertrand Joseph, 2022. "Autophagy regulation by RNA alternative splicing and implications in human diseases," Nature Communications, Nature, vol. 13(1), pages 1-17, 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:522:y:2015:i:7556:d:10.1038_nature14506. 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.