Calcium channels articles from across Nature Portfolio

L-type voltage-gated calcium channels are involved in multiple physiological functions. Here the authors identify calciseptine, a toxin purified from black mamba venom, as a selective inhibitor of Ca_v1.2 L-type Ca²⁺ channels.

TMEM63s are mechanosensitive ion channels activated by hypo-osmolality. Here, the authors determine the cryo-EM structure of mouse TMEM63C confirming its predominant monomeric state and the significance of TM0-TM6 coupling in channel activity.

The intermembrane complexes mediating calcium signals are crucial but poorly understood. Here the authors identify a Phe-His pair in the calcium-sensing STIM1 protein that controls both activation and pairing of STIM1 with Orai channels to generate calcium signals

Inositol 1,4,5-trisphosphate receptors (IP₃Rs) are intracellular Ca²⁺ channels that produce Ca²⁺ oscillations in response to GPCR and RTK activation. Here, Paknejad et al. resolve the conformational landscape of IP₃Rs that gives rise to the biphasic dependence on Ca²⁺ for channel activity.

Oxidation of ryanodine receptor calcium channels play a critical role in the onset of many cardiac diseases. Here, authors identify specific amino acids that cause ryanodine receptor malfunction during oxidative stress.

A study analyses the nanotopography of presynaptic calcium channels and release sensors and the degree of their coupling during maturation of an inhibitory synapse.

Gabapentinoids are first-line treatments for chronic pain but are associated with adverse side effects. A cryo-EM structure of gabapentin bound to its interaction site on the calcium channel α₂δ subunit now paves the way for the rational design of analgesics with greater selectivity and a reduced potential for adverse effects.

In this work, Morgenstern and colleagues describe an approach involving functionalized nanobodies which decrease the activity of voltage-gated Ca²⁺ channels associated with β₁ subunits and promote their removal from the surface membrane of neurons and muscle.