Thermosensitivity of the voltage-dependent activation of calcium homeostasis modulator 1 (calhm1) ion channel

Calcium homeostasis modulator 1 (calhm1) proteins form an outwardly rectifying nonselective ion channel having exceedingly slow kinetics and low sensitivity to voltage that is shifted by lowering extracellular Ca2+ ([Ca2+](e)). Here we found that physiological temperature dramatically facilitates the voltage-dependent activation of the calhm1 current (I-calhm1); increased amplitude (Q(10), 7-15) and fastened speed of activation. Also, the leftward shift of the half-activation voltage (V-1/2) was similary observed in the normal and lower [Ca2+](e). Since calhm1 is highly expressed in the brain and taste cells, the thermosensitivity should be considered in their electrophysiology. (C) 2020 Elsevier Inc. All rights reserved.

Automated summary

The study demonstrates that physiological temperature significantly enhances the activation of calhm1 current, resulting in increased amplitude, accelerated speed, and lower half-activation voltage. This finding is crucial for understanding the electrophysiology of brain and taste cells with high expression of calhm1.