scholarly journals An Ankyrin-G N-terminal Gate and Protein Kinase CK2 Dually Regulate Binding of Voltage-gated Sodium and KCNQ2/3 Potassium Channels

2015 ◽  
Vol 290 (27) ◽  
pp. 16619-16632 ◽  
Author(s):  
Mingxuan Xu ◽  
Edward C. Cooper
2008 ◽  
Vol 183 (6) ◽  
pp. 1101-1114 ◽  
Author(s):  
Aline Bréchet ◽  
Marie-Pierre Fache ◽  
Anna Brachet ◽  
Géraldine Ferracci ◽  
Agnés Baude ◽  
...  

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.


2003 ◽  
Vol 84 (2) ◽  
pp. 497-505 ◽  
Author(s):  
Yasuhiko Matsushita ◽  
Mayumi Ohshima ◽  
Kuniaki Yoshioka ◽  
Masamichi Nishiguchi ◽  
Hiroshi Nyunoya

2008 ◽  
Vol 312 (1-2) ◽  
pp. 61-69 ◽  
Author(s):  
Maciej Masłyk ◽  
Elżbieta Kochanowicz ◽  
Rafał Zieliński ◽  
Konrad Kubiński ◽  
Ulf Hellman ◽  
...  

FEBS Letters ◽  
1999 ◽  
Vol 462 (3) ◽  
pp. 353-357 ◽  
Author(s):  
Barbara Guerra ◽  
Stefan Siemer ◽  
Brigitte Boldyreff ◽  
Olaf-Georg Issinger

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