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Cover Image
Cover Image
Cover picture: Partial structural model of ENaC, an ion channel which functions as a pathway for Na+ transport across epithelia (αENaC, red; βENaC, blue; and γENaC, green). Conformational changes at interfaces between extracellular domain residues (shown in orange) participate in ENaC gating; movements that increase intersubunit distance favor the open state, whereas the closed state is favored when the distance is reduced (see research article by Collier et al., 337–348).
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Generally Physiological
Article
Knockout of the BK β2 subunit abolishes inactivation of BK currents in mouse adrenal chromaffin cells and results in slow-wave burst activity
Chromaffin cells from mice lacking the BK β2 subunit show decreased action potential firing during current injection but an increase in spontaneous burst firing.
Voltage-dependent regulation of CaV2.2 channels by Gq-coupled receptor is facilitated by membrane-localized β subunit
The pathway through which preferentially GqPCRs inhibit CaV2.2 channels depends on which β subunits are present.
A single amino acid substitution in CFTR converts ATP to an inhibitory ligand
The pathogenic G551D mutation of CFTR converts one of the two ATP-binding sites from excitatory to inhibitory.
Structure–activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects
The head and tail regions of 5-nitro-2-(3-phenylpropylamino)benzoate increase CFTR open probability through distinct mechanisms.
Intersubunit conformational changes mediate epithelial sodium channel gating
Residues forming interfaces between the three ENaC subunits participate in conformational changes required for transition between open and closed states.
