Palmitoylation-regulated interactions of the pseudokinase calmodulin kinase-like vesicle-associated with membranes and Arc/Arg3.1

Barbara Barylko, Per Niklas Hedde, Clinton A. Taylor, Derk D. Binns, Yu Kai Huang, Gemma Molinaro, Kimberly M Huber, David M. Jameson, Joseph P. Albanesi

Research output: Contribution to journalArticlepeer-review

Abstract

Calmodulin kinase-like vesicle-associated (CaMKv), a pseudokinase belonging to the Ca2+/calmodulin-dependent kinase family, is expressed predominantly in brain and neural tissue. It may function in synaptic strengthening during spatial learning by promoting the stabilization and enrichment of dendritic spines. At present, almost nothing is known regarding CaMKv structure and regulation. In this study we confirm prior proteomic analyses demonstrating that CaMKv is palmitoylated on Cys5. Wild-type CaMKv is enriched on the plasma membrane, but this enrichment is lost upon mutation of Cys5 to Ser. We further show that CaMKv interacts with another regulator of synaptic plasticity, Arc/Arg3.1, and that the interaction between these two proteins is weakened by mutation of the palmitoylated cysteine in CamKv.

Original languageEnglish (US)
Article number926570
JournalFrontiers in Synaptic Neuroscience
Volume14
DOIs
StatePublished - Jul 28 2022

Keywords

  • Arc-mCherry
  • Arc/Arg3.1
  • CaMKv
  • CaMKv-EGFP
  • palmitoylation
  • plasma membrane
  • pseudokinase

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology

Fingerprint

Dive into the research topics of 'Palmitoylation-regulated interactions of the pseudokinase calmodulin kinase-like vesicle-associated with membranes and Arc/Arg3.1'. Together they form a unique fingerprint.

Cite this