IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v458y2009i7237d10.1038_nature07961.html
   My bibliography  Save this article

The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins

Author

Listed:
  • Camilla Raiborg

    (Centre for Cancer Biomedicine, Norwegian Radium Hospital, University of Oslo
    Institute for Cancer Research, Rikshospitalet University Hospital)

  • Harald Stenmark

    (Centre for Cancer Biomedicine, Norwegian Radium Hospital, University of Oslo
    Institute for Cancer Research, Rikshospitalet University Hospital)

Abstract

Selective trafficking of membrane proteins to lysosomes for destruction is required for proper cell signalling and metabolism. Ubiquitylation aids this process by specifying which proteins should be transported to the lysosome lumen by the multivesicular endosome pathway. The endosomal sorting complex required for transport (ESCRT) machinery sorts cargo labelled with ubiquitin into invaginations of endosome membranes. Then, through a highly conserved mechanism also used in cytokinesis and viral budding, it mediates the breaking off of the cargo-containing intraluminal vesicles from the perimeter membrane. The involvement of the ESCRT machinery in suppressing diseases such as cancer, neurodegeneration and infections underscores its importance to the cell.

Suggested Citation

  • Camilla Raiborg & Harald Stenmark, 2009. "The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins," Nature, Nature, vol. 458(7237), pages 445-452, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07961
    DOI: 10.1038/nature07961
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07961
    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/nature07961?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. Tomoyuki Hatano & Saravanan Palani & Dimitra Papatziamou & Ralf Salzer & Diorge P. Souza & Daniel Tamarit & Mehul Makwana & Antonia Potter & Alexandra Haig & Wenjue Xu & David Townsend & David Rochest, 2022. "Asgard archaea shed light on the evolutionary origins of the eukaryotic ubiquitin-ESCRT machinery," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Sarah Renaud & Anthony Lefebvre & Olivier Moralès & Nadira Delhem, 2019. "Mini Review - Exosomes from Discovery to Isolation," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 15(2), pages 11286-11293, February.
    3. Jin-Xin Zheng & Tong-Yang Du & Guang-Can Shao & Zhu-Hui Ma & Zhao-Di Jiang & Wen Hu & Fang Suo & Wanzhong He & Meng-Qiu Dong & Li-Lin Du, 2023. "Ubiquitination-mediated Golgi-to-endosome sorting determines the toxin-antidote duality of fission yeast wtf meiotic drivers," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Meihua Jin & Hiroki Shiwaku & Hikari Tanaka & Takayuki Obita & Sakurako Ohuchi & Yuki Yoshioka & Xiaocen Jin & Kanoh Kondo & Kyota Fujita & Hidenori Homma & Kazuyuki Nakajima & Mineyuki Mizuguchi & Hi, 2021. "Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation," Nature Communications, Nature, vol. 12(1), pages 1-22, December.
    5. Yonglun Zeng & Baiying Li & Shuxian Huang & Hongbo Li & Wenhan Cao & Yixuan Chen & Guoyong Liu & Zhenping Li & Chao Yang & Lei Feng & Jiayang Gao & Sze Wan Lo & Jierui Zhao & Jinbo Shen & Yan Guo & Ca, 2023. "The plant unique ESCRT component FREE1 regulates autophagosome closure," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    6. Torben Mentrup & Anna Yamina Stumpff-Niggemann & Nadja Leinung & Christine Schlosser & Katja Schubert & Rebekka Wehner & Antje Tunger & Valentin Schatz & Patrick Neubert & Ann-Christine Gradtke & Jani, 2022. "Phagosomal signalling of the C-type lectin receptor Dectin-1 is terminated by intramembrane proteolysis," Nature Communications, Nature, vol. 13(1), pages 1-18, 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:458:y:2009:i:7237:d:10.1038_nature07961. 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.