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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
- 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.
- Subjects :
- Ankyrins
animal structures
[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Plasma protein binding
Biology
Article
Sodium Channels
Cell membrane
03 medical and health sciences
0302 clinical medicine
Ranvier's Nodes
medicine
Ankyrin
Animals
Protein kinase A
Casein Kinase II
Protein Kinase Inhibitors
Ion channel
Research Articles
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
Sodium channel
fungi
[SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Cell Biology
Axons
Cell biology
Rats
medicine.anatomical_structure
chemistry
Biochemistry
nervous system
Phosphorylation
Casein kinase 2
030217 neurology & neurosurgery
Protein Binding
Subjects
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⟩