IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v456y2008i7224d10.1038_nature07605.html
   My bibliography  Save this article

Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation

Author

Listed:
  • Rujun Kang

    (Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada)

  • Junmei Wan

    (Wayne State University School of Medicine, Detroit, Michigan 48201, USA)

  • Pamela Arstikaitis

    (Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada)

  • Hideto Takahashi

    (Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada)

  • Kun Huang

    (Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada)

  • Aaron O. Bailey

    (The Scripps Research Institute, La Jolla, California 10550, USA)

  • James X. Thompson

    (The Scripps Research Institute, La Jolla, California 10550, USA)

  • Amy F. Roth

    (Wayne State University School of Medicine, Detroit, Michigan 48201, USA)

  • Renaldo C. Drisdel

    (University of Chicago, Chicago, Illinois 60637, USA)

  • Ryan Mastro

    (University of Chicago, Chicago, Illinois 60637, USA)

  • William N. Green

    (University of Chicago, Chicago, Illinois 60637, USA)

  • John R. Yates III

    (The Scripps Research Institute, La Jolla, California 10550, USA)

  • Nicholas G. Davis

    (Wayne State University School of Medicine, Detroit, Michigan 48201, USA)

  • Alaa El-Husseini

    (Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada)

Abstract

Palmitoylation regulates diverse aspects of neuronal protein trafficking and function. Here a global characterization of rat neural palmitoyl-proteomes identifies most of the known neural palmitoyl proteins—68 in total, plus more than 200 new palmitoyl-protein candidates, with further testing confirming palmitoylation for 21 of these candidates. The new palmitoyl proteins include neurotransmitter receptors, transporters, adhesion molecules, scaffolding proteins, as well as SNAREs and other vesicular trafficking proteins. Of particular interest is the finding of palmitoylation for a brain-specific Cdc42 splice variant. The palmitoylated Cdc42 isoform (Cdc42-palm) differs from the canonical, prenylated form (Cdc42-prenyl), both with regard to localization and function: Cdc42-palm concentrates in dendritic spines and has a special role in inducing these post-synaptic structures. Furthermore, assessing palmitoylation dynamics in drug-induced activity models identifies rapidly induced changes for Cdc42 as well as for other synaptic palmitoyl proteins, suggesting that palmitoylation may participate broadly in the activity-driven changes that shape synapse morphology and function.

Suggested Citation

  • Rujun Kang & Junmei Wan & Pamela Arstikaitis & Hideto Takahashi & Kun Huang & Aaron O. Bailey & James X. Thompson & Amy F. Roth & Renaldo C. Drisdel & Ryan Mastro & William N. Green & John R. Yates II, 2008. "Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation," Nature, Nature, vol. 456(7224), pages 904-909, December.
    • Handle: RePEc:nat:nature:v:456:y:2008:i:7224:d:10.1038_nature07605
    DOI: 10.1038/nature07605
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07605
    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/nature07605?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:456:y:2008:i:7224:d:10.1038_nature07605. 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.