Modulation of low voltage-activated Cav3 T-type calcium channels remains poorly characterized compared with high voltage-activated Cav1 and Cav2 calcium channels. Notably, it is yet unresolved whether Cav3 channels are modulated by protein kinases in mammalian cells. In this study, we demonstrate that protein kinase A (PKA) and PKC (but not PKG) activation induces a potent increase in Cav3.1, Cav3.2, and Cav3.3 currents in various mammalian cell lines. Notably, we show that protein kinase effects occur at physiological temperature (∼30–37 °C) but not at room temperature (∼22–27 °C). This temperature dependence could involve kinase translocation, which is impaired at room temperature. A similar temperature dependence was observed for PKC-mediated increase in high voltage-activated Cav2.3 currents. We also report that neither Cav3 surface expression nor T-current macroscopic properties are modified upon kinase activation. In addition, we provide evidence for the direct phosphorylation of Cav3.2 channels by PKA in in vitro assays. Overall, our results clearly establish the role of PKA and PKC in the modulation of Cav3 T-channels and further highlight the key role of the physiological temperature in the effects described. [ABSTRACT FROM AUTHOR]