IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v465y2010i7300d10.1038_nature09076.html
   My bibliography  Save this article

Termination of autophagy and reformation of lysosomes regulated by mTOR

Author

Listed:
  • Li Yu

    (Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    School of Life Science, Tsinghua University
    State Key Laboratory of Biomembrane and Membrane Biotechnology, Beijing, 100084, China)

  • Christina K. McPhee

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    University of Maryland, College Park, Maryland 20742, USA)

  • Lixin Zheng

    (Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Gonzalo A. Mardones

    (Cell Biology and Metabolism Program, National Institute of Child Health & Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA
    Universidad Austral de Chile)

  • Yueguang Rong

    (School of Life Science, Tsinghua University
    State Key Laboratory of Biomembrane and Membrane Biotechnology, Beijing, 100084, China)

  • Junya Peng

    (School of Life Science, Tsinghua University
    State Key Laboratory of Biomembrane and Membrane Biotechnology, Beijing, 100084, China)

  • Na Mi

    (School of Life Science, Tsinghua University
    State Key Laboratory of Biomembrane and Membrane Biotechnology, Beijing, 100084, China)

  • Ying Zhao

    (Peking University Health Science Center, 38 Xueyuan Road, Beijing 100191, China)

  • Zhihua Liu

    (Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Fengyi Wan

    (Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Dale W. Hailey

    (Cell Biology and Metabolism Program, National Institute of Child Health & Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Viola Oorschot

    (University Medical Center Utrecht)

  • Judith Klumperman

    (University Medical Center Utrecht)

  • Eric H. Baehrecke

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA)

  • Michael J. Lenardo

    (Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA)

Abstract

mTOR and autophagy During autophagy, double-membrane autophagosomes sequester intracellular components and then fuse with lysosomes to form autolysosomes in which cargo is degraded. Under starvation conditions, the nutrient-responsive kinase, target of rapamycin (TOR), is inhibited, which results in an induction of autophagy. In this study, Yu et al. report a negative feedback mechanism by which lysosomes are reformed after the termination of autophagy. They demonstrate that upon prolonged starvation conditions, mTOR is reactivated, which attenuates autophagy and results in the formation of tubules and vesicles that extrude from autolysosomes. These mature into functional lysosomes, thereby restoring lysosome numbers in the cell. This feedback mechanism tightly couples nutritional status with the induction and termination of autophagy.

Suggested Citation

  • Li Yu & Christina K. McPhee & Lixin Zheng & Gonzalo A. Mardones & Yueguang Rong & Junya Peng & Na Mi & Ying Zhao & Zhihua Liu & Fengyi Wan & Dale W. Hailey & Viola Oorschot & Judith Klumperman & Eric , 2010. "Termination of autophagy and reformation of lysosomes regulated by mTOR," Nature, Nature, vol. 465(7300), pages 942-946, June.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7300:d:10.1038_nature09076
    DOI: 10.1038/nature09076
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09076
    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/nature09076?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. James L. Daly & Chris M. Danson & Philip A. Lewis & Lu Zhao & Sara Riccardo & Lucio Filippo & Davide Cacchiarelli & Daehoon Lee & Stephen J. Cross & Kate J. Heesom & Wen-Cheng Xiong & Andrea Ballabio , 2023. "Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Edoardo Ratto & S. Roy Chowdhury & Nora S. Siefert & Martin Schneider & Marten Wittmann & Dominic Helm & Wilhelm Palm, 2022. "Direct control of lysosomal catabolic activity by mTORC1 through regulation of V-ATPase assembly," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Hong Huang & Qinqin Ouyang & Min Zhu & Haijia Yu & Kunrong Mei & Rong Liu, 2021. "mTOR-mediated phosphorylation of VAMP8 and SCFD1 regulates autophagosome maturation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    4. Xinran Li & Cong Xiang & Shilei Zhu & Jiansheng Guo & Chang Liu & Ailian Wang & Jin Cao & Yan Lu & Dante Neculai & Pinglong Xu & Xin-Hua Feng, 2024. "SNX8 enables lysosome reformation and reverses lysosomal storage disorder," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    5. Alessia Calcagni’ & Leopoldo Staiano & Nicolina Zampelli & Nadia Minopoli & Niculin J. Herz & Giuseppe Tullio & Tuong Huynh & Jlenia Monfregola & Alessandra Esposito & Carmine Cirillo & Aleksandar Baj, 2023. "Loss of the batten disease protein CLN3 leads to mis-trafficking of M6PR and defective autophagic-lysosomal reformation," Nature Communications, Nature, vol. 14(1), pages 1-19, 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:465:y:2010:i:7300:d:10.1038_nature09076. 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.