IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-11686-9.html
   My bibliography  Save this article

A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD

Author

Listed:
  • Jennifer Schoberer

    (University of Natural Resources and Life Sciences, Vienna)

  • Julia König

    (University of Natural Resources and Life Sciences, Vienna)

  • Christiane Veit

    (University of Natural Resources and Life Sciences, Vienna)

  • Ulrike Vavra

    (University of Natural Resources and Life Sciences, Vienna)

  • Eva Liebminger

    (University of Natural Resources and Life Sciences, Vienna)

  • Stanley W. Botchway

    (Central Laser Facility, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Research Complex at Harwell)

  • Friedrich Altmann

    (University of Natural Resources and Life Sciences, Vienna)

  • Verena Kriechbaumer

    (Oxford Brookes University, Gipsy Lane, Headington)

  • Chris Hawes

    (Oxford Brookes University, Gipsy Lane, Headington)

  • Richard Strasser

    (University of Natural Resources and Life Sciences, Vienna)

Abstract

The Arabidopsis ER-α-mannosidase I (MNS3) generates an oligomannosidic N-glycan structure that is characteristically found on ER-resident glycoproteins. The enzyme itself has so far not been detected in the ER. Here, we provide evidence that in plants MNS3 exclusively resides in the Golgi apparatus at steady-state. Notably, MNS3 remains on dispersed punctate structures when subjected to different approaches that commonly result in the relocation of Golgi enzymes to the ER. Responsible for this rare behavior is an amino acid signal motif (LPYS) within the cytoplasmic tail of MNS3 that acts as a specific Golgi retention signal. This retention is a means to spatially separate MNS3 from ER-localized mannose trimming steps that generate the glycan signal required for flagging terminally misfolded glycoproteins for ERAD. The physiological importance of the very specific MNS3 localization is demonstrated here by means of a structurally impaired variant of the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1.

Suggested Citation

  • Jennifer Schoberer & Julia König & Christiane Veit & Ulrike Vavra & Eva Liebminger & Stanley W. Botchway & Friedrich Altmann & Verena Kriechbaumer & Chris Hawes & Richard Strasser, 2019. "A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11686-9
    DOI: 10.1038/s41467-019-11686-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-11686-9
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-019-11686-9?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
    ---><---

    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:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11686-9. 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.