Newest Articles
Optimization of FRET in mouse adult cardiomyocytesFRET-based biosensors are powerful tools to study intracellular signaling that require long culture times for adenoviral infection. Reddy et al. have developed a method for culturing adult mouse cardiomyocytes involving blebbistatin, which preserves cell morphology for up to 50 h after adenoviral infection.
Inactivation mechanism of BEST1BEST1 is a chloride channel that is activated by calcium. Vaisey and Long demonstrate that ionic currents through BEST1 inactivate by an allosteric mechanism in which the binding of a C-terminal peptide to a surface-exposed receptor controls a physically distant inactivation gate within the pore.
Stoichiometry of retigabine action on KCNQ channelsRetigabine is a widely studied potassium channel activator that is thought to interact with a conserved Trp side chain in the pore domain of Kv7 subunits. Yau et al. demonstrate that drug sensitivity in just one of the four subunits is sufficient for a near-maximal response to retigabine.
Stoichiometry of ICA-069673 action on KCNQ channelsKv7 potassium channels are strongly activated by a variety of small molecules with diverse mechanisms of action. Wang et al. investigate a compound that targets the voltage-sensing domain, ICA-069673, and demonstrate that four drug-sensitive subunits are required for maximal effect.
Detecting voltage sensitivity in membrane proteinsThe identification of voltage-sensing elements in membrane proteins is challenging due to the diversity of voltage-sensing mechanisms. Kasimova et al. present a computational approach to predict the elements involved in voltage sensing, which they validate using voltage-gated ion channels.
ENaC selectivityThe origin of ion selectivity in epithelial Na+ channels and the closely related acid-sensing ion channels is uncertain. Yang and Palmer show that the site of ion selectivity in epithelial Na+ channels is more extracellular than that proposed for acid-sensing ion channels.
STIM1 controls Orai1 gating and pore propertiesThe quantitative relation between STIM1 binding to Orai1 and store-operated CRAC channel activation is not well understood. Yen and Lewis find that STIM1 must bind to all six Orai1 subunits to effectively open the channel and generate the high ion selectivity and low conductance seen in native cells.
Current Issue
September 3, 2018
Volume 150, No. 9
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Reviews & Opinions
- Predicting voltage sensing
New method predicts the molecular basis of membrane proteins’ voltage sensitivity.
- Toward an understanding of the structural basis of allostery in muscarinic acetylcholine receptors
Burger et al. summarize our mechanistic understanding of allostery in the prototypical GPCR, the muscarinic acetylcholine receptor.
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Yeung and Prakriya highlight new research showing that STIM1 must bind to all six Orai1 subunits to effectively activate the channel.