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

doi:10.3389/fnsyn.2022.926570

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

Front Synaptic Neurosci. 2022 Jul 28:14:926570. doi: 10.3389/fnsyn.2022.926570. eCollection 2022.

Authors

Barbara Barylko¹, Per Niklas Hedde^{2

3}, Clinton A Taylor¹, Derk D Binns¹, Yu-Kai Huang³, Gemma Molinaro⁴, Kimberly M Huber⁴, David M Jameson², Joseph P Albanesi¹

Affiliations

¹ Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, United States.
² Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, United States.
³ Laboratory for Fluorescence Dynamics, University of California, Irvine, Irvine, CA, United States.
⁴ Department of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX, United States.

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.

Keywords: Arc-mCherry; Arc/Arg3.1; CaMKv; CaMKv-EGFP; palmitoylation; plasma membrane; pseudokinase.