IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v418y2002i6895d10.1038_nature00846.html
   My bibliography  Save this article

The C2B Ca2+-binding motif of synaptotagmin is required for synaptic transmission in vivo

Author

Listed:
  • J. M. Mackler

    (Colorado State University)

  • J. A. Drummond

    (University of Cambridge)

  • C. A. Loewen

    (Colorado State University)

  • I. M. Robinson

    (University of Cambridge)

  • N. E. Reist

    (Colorado State University)

Abstract

Synaptotagmin is a synaptic vesicle protein that is postulated to be the Ca2+ sensor for fast, evoked neurotransmitter release1. Deleting the gene for synaptotagmin (sytnull) strongly suppresses synaptic transmission in every species examined2, showing that synaptotagmin is central in the synaptic vesicle cycle. The cytoplasmic region of synaptotagmin contains two C2 domains, C2A and C2B. Five, highly conserved, acidic residues in both the C2A and C2B domains of synaptotagmin coordinate the binding of Ca2+ ions3,4,5, and biochemical studies have characterized several in vitro Ca2+-dependent interactions between synaptotagmin and other nerve terminal molecules6. But there has been no direct evidence that any of the Ca2+-binding sites within synaptotagmin are required in vivo. Here we show that mutating two of the Ca2+-binding aspartate residues in the C2B domain (D416,418N in Drosophila) decreased evoked transmitter release by >95%, and decreased the apparent Ca2+ affinity of evoked transmitter release. These studies show that the Ca2+-binding motif of the C2B domain of synaptotagmin is essential for synaptic transmission.

Suggested Citation

  • J. M. Mackler & J. A. Drummond & C. A. Loewen & I. M. Robinson & N. E. Reist, 2002. "The C2B Ca2+-binding motif of synaptotagmin is required for synaptic transmission in vivo," Nature, Nature, vol. 418(6895), pages 340-344, July.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6895:d:10.1038_nature00846
    DOI: 10.1038/nature00846
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature00846
    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/nature00846?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. Kevin C. Courtney & Taraknath Mandal & Nikunj Mehta & Lanxi Wu & Yueqi Li & Debasis Das & Qiang Cui & Edwin R. Chapman, 2023. "Synaptotagmin-7 outperforms synaptotagmin-1 to promote the formation of large, stable fusion pores via robust membrane penetration," Nature Communications, Nature, vol. 14(1), pages 1-15, 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:418:y:2002:i:6895:d:10.1038_nature00846. 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.