IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v466y2010i7310d10.1038_nature09296.html
   My bibliography  Save this article

A ribosome-associating factor chaperones tail-anchored membrane proteins

Author

Listed:
  • Malaiyalam Mariappan

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Xingzhe Li

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
    School of Basic Medical Sciences, Peking University)

  • Sandra Stefanovic

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Ajay Sharma

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Agnieszka Mateja

    (929 East 57th Street, University of Chicago)

  • Robert J. Keenan

    (929 East 57th Street, University of Chicago)

  • Ramanujan S. Hegde

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

Abstract

Bat3: a chaperone to TA proteins Tail-anchored (TA) proteins have a single transmembrane domain at their C-termini and are post-translationally targeted to the endoplasmic reticulum via the cytosolic ATPase, TRC40. In this study, Mariappan et al. identify a conserved protein complex called Bat3 complex that is recruited to ribosomes and interacts with the transmembrane domain of newly released TA proteins, transferring them to TRC40 for subsequent targeting to the endoplasmic reticulum. Thus the Bat3 complex functions as a transmembrane-domain-specific chaperone that channels TA proteins to the TRC40 insertion pathway.

Suggested Citation

  • Malaiyalam Mariappan & Xingzhe Li & Sandra Stefanovic & Ajay Sharma & Agnieszka Mateja & Robert J. Keenan & Ramanujan S. Hegde, 2010. "A ribosome-associating factor chaperones tail-anchored membrane proteins," Nature, Nature, vol. 466(7310), pages 1120-1124, August.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7310:d:10.1038_nature09296
    DOI: 10.1038/nature09296
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09296
    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/nature09296?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:466:y:2010:i:7310:d:10.1038_nature09296. 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.