IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v391y1998i6663d10.1038_34438.html
   My bibliography  Save this article

COPII–cargo interactions direct protein sorting into ER-derived transport vesicles

Author

Listed:
  • Meta J. Kuehn

    (Barker Hall, Howard Hughes Medical Institute, University of California)

  • Johannes M. Herrmann

    (Barker Hall, Howard Hughes Medical Institute, University of California)

  • Randy Schekman

    (Barker Hall, Howard Hughes Medical Institute, University of California)

Abstract

Vesicles coated with coat protein complex II (COPII) selectively transport molecules (cargo) and vesicle fusion proteins from the endoplasmic reticulum (ER) to the Golgi complex1,2,3. We have investigated the role of coat proteins in cargo selection and recruitment. We isolated integral membrane and soluble cargo proteins destined for transport from the ER in complexes formed in the presence of Sar1 and Sec23/24, a subset of the COPII components, and GTP or GMP-PNP. Vesicle fusion proteins of the vSNARE family and Emp24, a member of a putative cargo carrier family4, were also found in COPII complexes. The inclusion of amino-acid permease molecules into the complex depended on the presence of Shr3, a protein required for the permease to leave the ER3,5. Resident ER proteins Sec61, BiP (Kar2) and Shr3 were not included in the complexes, indicating that the COPII components bound specifically to vesicle cargo. COPII–cargo complexes and putative cargo adaptor–cargo complexes were also isolated from COPII vesicles. Our results indicate that cargo packaging signals and soluble cargo adaptors are recognized by a recruitment complex comprising Sar1–GTP and Sec23/24.

Suggested Citation

  • Meta J. Kuehn & Johannes M. Herrmann & Randy Schekman, 1998. "COPII–cargo interactions direct protein sorting into ER-derived transport vesicles," Nature, Nature, vol. 391(6663), pages 187-190, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6663:d:10.1038_34438
    DOI: 10.1038/34438
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/34438
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/34438?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. Cathena Meiling Li & Jaemin Kang & Jongyeon Baek & Youbin Kim & Heemin Park & Yong-Keun Jung, 2024. "Cytosolic FKBPL and ER-resident CKAP4 co-regulates ER-phagy and protein secretion," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Julia D. Knopf & Susanne S. Steigleder & Friederike Korn & Nathalie Kühnle & Marina Badenes & Marina Tauber & Sebastian J. Theobald & Jan Rybniker & Colin Adrain & Marius K. Lemberg, 2024. "RHBDL4-triggered downregulation of COPII adaptor protein TMED7 suppresses TLR4-mediated inflammatory signaling," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. William Kasberg & Peter Luong & Kevin A. Swift & Anjon Audhya, 2023. "Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport," Nature Communications, Nature, vol. 14(1), pages 1-13, 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:391:y:1998:i:6663:d:10.1038_34438. 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.