Referenced in: none

Automatically associated channels: Cav2.2

Title: Cdk5-mediated phosphorylation of CRMP-2 enhances its interaction with CaV2.2.

Authors: Joel M Brittain, Yuying Wang, Omotore Eruvwetere, Rajesh Khanna

Journal, date & volume: FEBS Lett., 2012 Nov 2 , 586, 3813-8

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/23022559

Abstract
The axon/dendrite specification collapsin response mediator protein-2 (CRMP-2) bidirectionally regulates N-type voltage-gated Ca(2+) channels (CaV2.2). But how cyclin dependent kinase 5 (Cdk5)-mediated phosphorylation of CRMP-2 affects its interaction/regulation with CaV2.2 is unknown. CRMP-2-mediated enhancement of currents via CaV2.2 was not observed with a Cdk5 phospho-null CRMP-2-S522A mutant or in cells expressing an inactive Cdk5. Concomitant knockdown of endogenous CRMP2 and overexpression of CRMP2-S522A mutant refractory to knockdown phenocopied the reduction in Ca(2+) influx while the Rho kinase CRMP2-T555A mutant was ineffective. Cdk5-phosphorylated CRMP-2 had increased association with CaV2.2. These results identify an important role for Cdk5 in CRMP2-mediated CaV2.2 regulation.