Key result
A de novo mutation in the Kv3.1 potassium channel causing early-onset epilepsy prevents phosphorylation by protein kinase C, despite having identical properties to wild-type channels.
A de novo mutation in the Kv3.1 potassium channel causes epilepsy by preventing phosphorylation by protein kinase C, highlighting the role of channel modulation in normal brain function.
Kv3.1 modulation defects may underlie epilepsy with intellectual disability; leaves open whether targeting phosphorylation offers therapeutic avenues.
Ion channel mutations that cause serious human diseases generally alter the biophysical properties or expression of the channel. We describe a de novo mutation in the Kv3.1 potassium channel that causes severe intellectual disability with early-onset epilepsy. The properties of this channel appear identical to those of wild-type channels, but the mutation prevents phosphorylation of the channel by protein kinase C. Our findings emphasize the role of channel modulation in normal brain function.
No takes yet. Share an insight, caveat, or question.
Zhang et al. (2021) studied Epilepsy of infancy with focal migrating seizures. KCNC1 mutation vs. Wild-type channels was evaluated on Phosphorylation of the channel by protein kinase C. A de novo mutation in the Kv3.1 potassium channel causing early-onset epilepsy prevents phosphorylation by protein kinase C, despite having identical properties to wild-type channels.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: