Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation

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, Nicholas G. Davis () and Alaa El-Husseini
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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: 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

Nature, 2008, vol. 456, issue 7224, 904-909

Abstract: 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.

Date: 2008
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DOI: 10.1038/nature07605

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