1. Department of Psychiatry, Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada
2. Department of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA
3. Department of Cell Biology, The Scripps Research Institute, La Jolla, California 10550, USA
4. Department of Neurobiology, University of Chicago, Chicago, Illinois 60637, USA
5. These authors contributed equally to this work.
6. Deceased.

Correspondence to: Rujun Kang^1,5Nicholas G. Davis^2,5 Correspondence and requests for materials should be addressed to N.G.D. (Email: ndavis@med.wayne.edu) or R.K (Email: rkang@interchange.ubc.ca).

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.

MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.