The Rockefeller University Press $30.00 J. Gen. Physiol. 2016 Vol. 148 No. 3 201–205 www.jgp.org/cgi/doi/10.1085/jgp.201611671 201 Inwardly rectifying potassium (Kir) channels are important regulators of cellular excitability, enabling cells to alter electrical activity in response to diverse autonomic and metabolic signals (Hibino et al., 2010). Fairly or not, the Kir channel family is sometim...

The Rockefeller University Press $30.00 J. Gen. Physiol. 2016 Vol. 148 No. 3 201–205 www.jgp.org/cgi/doi/10.1085/jgp.201611671 201 Inwardly rectifying potassium (Kir) channels are important regulators of cellular excitability, enabling cells to alter electrical activity in response to diverse autonomic and metabolic signals (Hibino et al., 2010). Fairly or not, the Kir channel family is sometim...

The Rockefeller University Press $30.00 J. Gen. Physiol. 2016 Vol. 148 No. 3 201–205 www.jgp.org/cgi/doi/10.1085/jgp.201611671 201 Inwardly rectifying potassium (Kir) channels are important regulators of cellular excitability, enabling cells to alter electrical activity in response to diverse autonomic and metabolic signals (Hibino et al., 2010). Fairly or not, the Kir channel family is sometim...

We have found that phosphorylation of a G-protein-coupled receptor by protein kinase C (PKC) disrupts modulation of ion channels by the receptor. In AtT-20 cells transfected with rat cannabinoid receptor (CB1), the activation of an inwardly rectifying potassium current (Kir current) and depression of P/Q-type calcium channels by cannabinoids were prevented by stimulation of protein kinase C by ...

Inward rectifier K(+) (Kir) channels play an important role in forming membrane potential and then modulating muscle tone in certain types of smooth muscles. In cultured human bronchial smooth muscle cells (hBSMCs), Kir current was identified using whole-cell voltage clamp techniques and explored by using RT-PCR analysis of mRNA, Western blotting, and antisense oligonucleotide methods to block ...

KirBac1.1 is a prokaryotic homologue of eukaryotic inward rectifier potassium (Kir) channels. The crystal structure of KirBac1.1 and related KirBac3.1 have now been used extensively to generate in silico models of eukaryotic Kir channels, but functional analysis has been limited to (86)Rb(+) flux experiments and bacteria or yeast complementation screens, and no voltage clamp analysis has been a...

Inhibition by intracellular H(+) (pH gating) and activation by phosphoinositides such as PIP(2) (PIP(2)-gating) are key regulatory mechanisms in the physiology of inwardly-rectifying potassium (Kir) channels. Our recent findings suggest that PIP(2) gating and pH gating are controlled by an intra-subunit H-bond at the helix-bundle crossing between a lysine in TM1 and a backbone carbonyl group in...

Inward-rectifier K(+) (Kir) channels play many important biological roles and are emerging as important therapeutic targets. Subtype-specific inhibitors would be useful tools for studying the channels' physiological functions. Unfortunately, available K(+) channel inhibitors generally lack the necessary specificity for their reliable use as pharmacological tools to dissect the various kinds of ...