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Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G

Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G

Authors :
Agnès Baude
Anna Brachet
Bénédicte Dargent
Géraldine Ferracci
Aline Brechet
Christophe Leterrier
Marie-Pierre Fache
Sandrine Pereira
Marie Irondelle
Leterrier, Christophe
Neurobiologie des Canaux Ioniques
Université de la Méditerranée - Aix-Marseille 2-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M)
Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de la Méditerranée - Aix-Marseille 2
Source :
Journal of Cell Biology, Journal of Cell Biology, 2008, 183 (6), pp.1101-1114. ⟨10.1083/jcb.200805169⟩, The Journal of Cell Biology, Journal of Cell Biology, Rockefeller University Press, 2008, 183 (6), pp.1101-1114. ⟨10.1083/jcb.200805169⟩
Publication Year :
2008
Publisher :
HAL CCSD, 2008.

Abstract

In neurons, generation and propagation of action potentials requires the precise accumulation of sodium channels at the axonal initial segment (AIS) and in the nodes of Ranvier through ankyrin G scaffolding. We found that the ankyrin-binding motif of Nav1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Nav channel interaction with ankyrins. Furthermore, we observed that CK2 is highly enriched at the AIS and the nodes of Ranvier in vivo. An ion channel chimera containing the Nav1.2 ankyrin-binding motif perturbed endogenous sodium channel accumulation at the AIS, whereas phosphorylation-deficient chimeras did not. Finally, inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G.

Details

Language :
English
ISSN :
00219525 and 15408140
Database :
OpenAIRE
Journal :
Journal of Cell Biology, Journal of Cell Biology, 2008, 183 (6), pp.1101-1114. ⟨10.1083/jcb.200805169⟩, The Journal of Cell Biology, Journal of Cell Biology, Rockefeller University Press, 2008, 183 (6), pp.1101-1114. ⟨10.1083/jcb.200805169⟩
Accession number :
edsair.doi.dedup.....e09b13678e099cfc39f9394667662880
Full Text :
https://doi.org/10.1083/jcb.200805169⟩