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.