TRPM8 channels are a polymodal receptors activated by voltage, low temperatures and agonists. The structural data suggests that the distal C-terminus (1064-1104 amino acid residues) form a coiled-coil motif. Our aim was to investigate the importance of this structure in the thermo-sensitivity of TRPM8. TRPM8 wild type and deletion mutants of the coiled-coil region of this channel were cloned and expressed in Xenopus oocytes. Macroscopic currents were recorded by patch-clamp technique in cell-attached configuration at different temperatures (10°C- 40°C). An analysis of the conductance-voltage curves determined from tail currents showed that values of the voltage at which the open probability is 0,5 (V1/2 ) saturate at high and low temperatures. These results and limiting slope analysis of the open probability-voltage curves demonstrated that TRPM8 channel gating is best explained using an allosteric gating model for both voltage and temperature dependence. On the other hand, gradual deletions of the coiled-coil region (from 1064 to 1104 residues) promoted a gradual decrease in the temperature sensitivity of TRPM8 channel, without affecting the voltage dependence. The decrease in the enthalpy promoted by gradual deletions of the distal C-terminus suggests that coiled-coil region is a structural determinant of the thermo sensitivity in TRPM8 channels. Our results also indicate that the voltage and temperature sensors are localized in different structural domains.