Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.
Charybdotoxin, a toxin produced by scorpions, blocks a K+ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K+ mimic in the selectivity filter.
The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.
Detection of unbinding transitional states in the charybdotoxin first-order dissociation from a Kv-channel reveals that the bound neurotoxin wobbles, suggesting diverse intermediates and dissociation pathways in this protein–protein interaction.
ZDHHC14 controls palmitoylation and axon initial segment targeting of PSD93 and Kv1-family potassium channels, events that are essential for normal neuronal excitability.
The sodium leak NALCN channel functions as a core effector of GABA-B and D2 receptors that is used along with GIRK channels to regulate action potential firing in dopamine neurons.
The contribution of biophysical ion channels to neuron function can be predicted by taking advantage of an ongoing dialogue between model and experiment.
A mouse model of human muscle myopathy is used to provide mechanistic insight, identify possible biomarkers of disease, and suggest possible therapeutic strategies to alleviate muscle weakness.
