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Tetrodotoxin-resistant voltage-gated sodium channel Na v 1.8 constitutively interacts with ankyrin G

Abstract : The tetrodotoxin-resistant (TTX-R) voltage-gated sodium channel Na v 1.8 is predominantly expressed in peripheral afferent neurons, but in case of neuronal injury an ectopic and detrimental expression of Na v 1.8 occurs in neurons of the CNS. In CNS neurons, Na v 1.2 and Na v 1.6 channels accumulate at the axon initial segment, the site of the generation of the action potential, through a direct interaction with the scaffolding protein ankyrin G (ankG). This interaction is regulated by protein kinase CK2 phosphorylation. In this study, we quantitatively analyzed the interaction between Na v 1.8 and ankG. GST pull-down assay and surface plasmon resonance technology revealed that Na v 1.8 strongly and constitutively interacts with ankG, in comparison to what observed for Na v 1.2. An ion channel bearing the ankyrin-binding motif of Na v 1.8 displaced the endogenous Na v 1 accumulation at the axon initial segment of hippocampal neurons. Finally, Na v 1.8 and ankG co-localized in skin nerves fibers. Altogether, these results indicate that Na v 1.8 carries all the information required for its localization at ankG micro-domains. The constitutive binding of Na v 1.8 with ankG could contribute to the pathological aspects of illnesses where Na v 1.8 is ectopically expressed in CNS neurons.
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https://hal.archives-ouvertes.fr/hal-01772912
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Submitted on : Tuesday, April 24, 2018 - 12:06:32 PM
Last modification on : Friday, October 22, 2021 - 3:35:51 AM

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Audrey Montersino, Anna Brachet, Geraldine Ferracci, Marie-Pierre Fache, Stephanie Angles d'Ortoli, et al.. Tetrodotoxin-resistant voltage-gated sodium channel Na v 1.8 constitutively interacts with ankyrin G. Journal of Neurochemistry, Wiley, 2014, 131 (1), pp.33-41. ⟨10.1111/jnc.12785⟩. ⟨hal-01772912⟩

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