Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Kang, R. J.
  • Wan, J. M.
  • Arstikaitis, P.
  • Takahashi, H.
  • Huang, K.
  • Bailey, A. O.
  • Thompson, J. X.
  • Roth, A. F.
  • Drisdel, R. C.
  • Mastro, R.
  • Green, W. N.
  • Yates III, John
  • Davis, N. G.
  • El-Husseini, A.

publication date

  • December 2008

journal

  • Nature  Journal

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.

subject areas

  • Alternative Splicing
  • Animals
  • Cells, Cultured
  • Cerebral Cortex
  • Dendrites
  • Lipoylation
  • Models, Neurological
  • Neurons
  • Organ Specificity
  • Proteome
  • Proteomics
  • Rats
  • Synapses
  • cdc42 GTP-Binding Protein
scroll to property group menus

Identity

PubMed Central ID

  • PMC2610860

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/nature07605

PubMed ID

  • 19092927
scroll to property group menus

Additional Document Info

start page

  • 904

end page

  • 909

volume

  • 456

issue

  • 7224

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support