IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v519y2015i7544d10.1038_nature14107.html
   My bibliography  Save this article

SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

Author

Listed:
  • Manuele Rebsamen

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Lorena Pochini

    (Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)

  • Taras Stasyk

    (Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)

  • Mariana E. G. de Araújo

    (Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)

  • Michele Galluccio

    (Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)

  • Richard K. Kandasamy

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Berend Snijder

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Astrid Fauster

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Elena L. Rudashevskaya

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
    Present address: Institute of Medical Chemistry, Medical University of Vienna, 1090 Vienna, Austria.)

  • Manuela Bruckner

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Stefania Scorzoni

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Przemyslaw A. Filipek

    (Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)

  • Kilian V. M. Huber

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Johannes W. Bigenzahn

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Leonhard X. Heinz

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Claudine Kraft

    (Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria)

  • Keiryn L. Bennett

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

  • Cesare Indiveri

    (Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)

  • Lukas A. Huber

    (Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)

  • Giulio Superti-Furga

    (CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)

Abstract

The mTORC1 protein kinase complex integrates nutrient and growth stimuli to modulate signalling pathways that regulate cellular metabolism and physiology, but the molecular nature of the amino acid sensing mechanism at the lysosome is unknown; here, an orphan member of the human solute carrier group of proteins, SLC38A9, is shown to be an integral component of the lysosomal machinery that can directly sense amino acids and activate mTORC1.

Suggested Citation

  • Manuele Rebsamen & Lorena Pochini & Taras Stasyk & Mariana E. G. de Araújo & Michele Galluccio & Richard K. Kandasamy & Berend Snijder & Astrid Fauster & Elena L. Rudashevskaya & Manuela Bruckner & St, 2015. "SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1," Nature, Nature, vol. 519(7544), pages 477-481, March.
  • Handle: RePEc:nat:nature:v:519:y:2015:i:7544:d:10.1038_nature14107
    DOI: 10.1038/nature14107
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14107
    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/nature14107?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. Lior Artzi & Assaf Alon & Kelly P. Brock & Anna G. Green & Amy Tam & Fernando H. Ramírez-Guadiana & Debora Marks & Andrew Kruse & David Z. Rudner, 2021. "Dormant spores sense amino acids through the B subunits of their germination receptors," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    2. Zhenzhen Zi & Zhuzhen Zhang & Qiang Feng & Chiho Kim & Xu-Dong Wang & Philipp E. Scherer & Jinming Gao & Beth Levine & Yonghao Yu, 2022. "Quantitative phosphoproteomic analyses identify STK11IP as a lysosome-specific substrate of mTORC1 that regulates lysosomal acidification," Nature Communications, Nature, vol. 13(1), pages 1-12, 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:519:y:2015:i:7544:d:10.1038_nature14107. 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.