IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v419y2002i6904d10.1038_nature01040.html
   My bibliography  Save this article

Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat

Author

Listed:
  • Xiping Bi

    (Memorial Sloan-Kettering Cancer Center)

  • Richard A. Corpina

    (Memorial Sloan-Kettering Cancer Center)

  • Jonathan Goldberg

    (Memorial Sloan-Kettering Cancer Center)

Abstract

COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1–GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24–Sar1 complex reveals a bow-tie-shaped structure, 15 nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis.

Suggested Citation

  • Xiping Bi & Richard A. Corpina & Jonathan Goldberg, 2002. "Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat," Nature, Nature, vol. 419(6904), pages 271-277, September.
    • Handle: RePEc:nat:nature:v:419:y:2002:i:6904:d:10.1038_nature01040
    DOI: 10.1038/nature01040
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature01040
    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/nature01040?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.

    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:419:y:2002:i:6904:d:10.1038_nature01040. 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.