Literature DB >> 23022559

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

Joel M Brittain1, Yuying Wang, Omotore Eruvwetere, Rajesh Khanna.   

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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2012        PMID: 23022559     DOI: 10.1016/j.febslet.2012.09.022

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  41 in total

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