Ca_v1.2 channel phosphorylation plays an important role in regulating neuronal plasticity by action potential-dependent Ca²⁺ entry. Most studies of Ca_v1.2 regulation by phosphorylation have been reported in heart and muscles. Here, we identified phosphorylation sites of neuronal Ca_v1.2 channel protein purified from rat brain using mass spectrometry. The functional characterization of these phosphorylation sites showed altered voltage-dependent biophysical properties of the channel, without affecting current density. These results show that neuronal Ca_v1.2 channel is regulated by phosphorylation in a complex mechanism involving multiple phosphorylation sites.

Ca _{v 1.2 通道磷酸化在通过动作电位依赖性Ca} ²⁺进入调节神经元可塑性中起重要作用。大多数关于通过磷酸化调节 Ca _v 1.2 的研究已在心脏和肌肉中报道。在这里，我们使用质谱法鉴定了从大鼠脑中纯化的神经元 Ca _{v 1.2 通道蛋白的磷酸化位点。}这些磷酸化位点的功能表征显示通道的电压依赖性生物物理特性发生了改变，而不会影响电流密度。这些结果表明神经元 Ca _v 1.2 通道在涉及多个磷酸化位点的复杂机制中受到磷酸化的调节。