Millet et al. show that the C. elegans orthologue of the PIEZO family, PEZO-1, is a mechanosensitive ion channel involved in food sensation and in regulating pharyngeal function in the nematode.

Chen et al. computationally model the open conformation of the hASIC1a channel to predict that mutations that eliminate channel selectivity cause a widening of the GAS belt. Their findings implicate the GAS belt diameter in channel kinetics and ion selectivity.

Albadrani et al. studied the potential of angiotensin 1–7 to prevent the atrophy that normally ensues muscle denervation. Increasing angiotensin 1–7 levels do not prevent muscle mass loss in denervated muscles but maintain normalized tetanic force to cross-sectional area and membrane excitability for up to 28 d.

Morris et al. use a computational model of Pump-Leak/Donnan ion homeostasis to suggest that the Donnan dominated steady-state of skeletal muscle fibers underpins their longevity in the face of the structural and metabolic injuries incurred with Duchenne muscular dystrophy.

Angelini et al. show that reducing late L-type Ca2+ current with the purine analogue roscovitine is sufficient to suppress ventricular arrhythmias in myocytes and ex vivo hearts. By preserving the early component of ICa,L, this strategy is expected to largely maintain contractility, an advantage over Ca2+ channel blockers.

Desplat et al. show that the Piezo1 channel mediates Ca2+ entry into mouse cholangiocytes as a result of mechanical stress due to cell swelling. Piezo1 thus activates and forms complexes with Pannexin1, which result in force-induced ATP release and signal amplification through P2X4R.

Jaque-Fernández et al. show that downregulation of CaV1.1 in muscle fibers elevates ATP release, whereas downregulation of Panx1 depresses depolarization-induced intracellular Ca2+ release. They conclude that Panx1 is a reciprocal partner of CaV1.1 for both excitation–contraction and excitation–transcription coupling.