Sodium taste, a distinct taste modality induced by sodium ions (Na⁺), elicits attraction to sodium salts, and thereby regulates the amount of salt consumption. The amiloride-sensitive epithelial sodium channel (ENaC) is the Na⁺ sensor located in the apical membranes of taste cells dedicated to sodium taste, which we can refer to as sodium cells. However, the identity of sodium cells, their intracellular signaling cascade, and neurotransmission mechanism remain long-standing enigmas. In this study, we show that a subset of taste cells with ENaC activity fire action potentials in response to ENaC-mediated Na⁺ influx without changing the intracellular Ca²⁺ concentration, and form an atypical chemical synapse with afferent neurons involving the voltage-gated ion channel CALHM1/3 as the conduit for neurotransmitter release, which we have termed the "channel synapse". Genetic elimination of ENaC in Calhm1-expressing cells (ENaC cKO) as well as global Calhm3 knockout (KO) abolished the amiloride-sensitive component of the gustatory nerve responses and attenuated behavioral attraction to NaCl. Together, cells expressing ENaC and CALHM1/3 constitute sodium cells, where the entry of oral Na⁺ elicits suprathreshold depolarization for action potentials driving voltage-dependent neurotransmission via the channel synapse. Thus, from the sensor to neurotransmission process, sodium taste signaling bypasses Ca²⁺ signals by involving only Ca²⁺-independent ion channels: ENaC, voltage-gated Na⁺ channels, and CALHM1/3.