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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
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    Cited by:

    1. Xiaotian Zhang & Heykyeong Jeong & Jingwen Niu & Sabrina M. Holland & Brittany N. Rotanz & John Gordon & Margret B. Einarson & Wayne E. Childers & Gareth M. Thomas, 2025. "Inhibiting acute, axonal DLK palmitoylation is neuroprotective and avoids deleterious effects of cell-wide DLK inhibition," Nature Communications, Nature, vol. 16(1), pages 1-19, December.

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