- Secondary anionic lipid site in Kir2 channels
Phospholipids are required to bind to two distinct sites on the inward rectifier potassium channel for maximal efficacy. Lee et al. show that a membrane-associating tryptophan residue in the second site can mimic the effect of phospholipid binding and cause a conformational change to reveal the primary binding site.
- Renal Cl− channel: Regulation by voltage and pH
ClC-K2 is present on the basolateral membrane of kidney epithelial cells, but little is known about its single channel properties. Pinelli et al. record unitary ClC-K2 currents from intercalated cells of mouse connecting tubules and investigate their regulation by voltage, pH, Cl−, and Ca2+.
- The α2δ-1 subunit remodels CaV1.2 voltage sensors
Voltage-sensing domains (VSDs) in voltage-gated calcium channels sense the potential difference across membranes and interact with the pore to open it. Savalli et al. find that the accessory subunit α2δ-1 increases the sensitivity of VSDs I–III and also their efficiency of coupling to the pore.
- Ion channel coupling in epithelial ion transport
Principal cells regulate the ionic environment of the epididymal lumen via unknown mechanisms. Gao et al. use electrophysiological and pharmacological tools to characterize rat principal cells and reveal a TRPV6-mediated calcium conductance and TMEM16A-mediated calcium-activated chloride conductance.
- AmCaV4 channel characterization
Insect DSC1 channels have sequences that are intermediate between voltage-gated Na+ and Ca2+ channels but have hitherto been classified as the former. Gosselin-Badaroudine et al. clone and characterize honeybee DSC1, revealing high selectivity for Ca2+ and suggesting reclassification of DSC1 homologues as Ca2+ channels.
- Conformational heterogeneity of KcsA in bicelles
KcsA is a potassium channel that is gated open and closed by changes in pH. Kim et al. find that at least two conformational states exist for both closed and open KcsA channels using solution NMR.