Approaches from information theory and probabilistic modeling show that voltage-sensing domain sequences conform to a small set of rules.
The molecular strategy for alkali cation selectivity by a bacterial sodium channel resembles those of eukaryotic calcium and potassium channels, rather than those of eukaryotic sodium channels.
Introduction of charged residues into the voltage sensor provides insight into the molecular mechanisms underlying potassium channel sensitivity to polyunsaturated fatty acids.
Phosphatidylinositol 4,5-bisphosphate has a direct role in regulating receptor-operated TRPC channel activation and inactivation.
UV light stimulates a phosphoinositide signaling pathway in human melanocytes similar to those elicited by light in the eye.
Removal of immunoglobulin-like domains from titin’s spring segment alters titin splicing in mouse skeletal muscle and causes myopathy
Changes in titin splicing resulting in decreased size and increased stiffness lead to pathological changes in skeletal muscle.
Calcium-dependent stoichiometries of the KCa2.2 (SK) intracellular domain/calmodulin complex in solution
Biophysical analyses indicate that the Ca2+-activated K+ channel SK2 binds calmodulin with multiple stoichiometries, distinct from the two SK2-two calmodulin stoichiometry identified by crystallography.
Calcium-mediated activation of the TMEM16A chloride channel does not depend on changes in phosphorylation status or the calcium-binding protein calmodulin.
Catalyst-like modulation of transition states for CFTR channel opening and closing: New stimulation strategy exploits nonequilibrium gating
Two gating transition states determine open probability of CFTR (the chloride channel mutated in cystic fibrosis), defining strategic targets for therapeutic intervention.
Aromatic–aromatic interactions between residues in KCa3.1 pore helix and S5 transmembrane segment control the channel gating process
Interactions between aromatic amino acid residues in the pore helix and S5 transmembrane domain control gating of the Ca2+-activated potassium channel KCa3.1.