Saimi Y, Kung C
Laboratory of Molecular Biology, University of Wisconsin, Madison.
FEBS Lett. 1994 Aug 22;350(2-3):155-8. doi: 10.1016/0014-5793(94)00782-9.
While many ion channels are modulated by phosphorylation, there is growing evidence that they can also be regulated by Ca(2+)-calmodulin, apparently through direct binding. In some cases, this binding activates channels; in others, it modulates channel activities. These phenomena have been documented in Paramecium, in Drosophila, in vertebrate photoreceptors and olfactory receptors, as well as in ryanodine receptor Ca(2+)-release channels. Furthermore, studies on calmodulin mutants in Paramecium have shown a clear bipartite distribution of two groups of mutations in the calmodulin gene that lead to opposite behavioral and electrophysiological phenotypes. These results indicate that the N-lobe of calmodulin specifically interacts with one class of ion-channel proteins and the C-lobe with another.
虽然许多离子通道受磷酸化调节，但越来越多的证据表明，它们也可由Ca(2+)-钙调蛋白调节，显然是通过直接结合。在某些情况下，这种结合会激活通道；在其他情况下，则会调节通道活性。这些现象已在草履虫、果蝇、脊椎动物光感受器和嗅觉感受器以及兰尼碱受体Ca(2+)-释放通道中得到记录。此外，对草履虫钙调蛋白突变体的研究表明，钙调蛋白基因中的两组突变呈现明显的两部分分布，导致相反的行为和电生理表型。这些结果表明，钙调蛋白的N端叶与一类离子通道蛋白特异性相互作用，C端叶与另一类相互作用。
