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lüll Ion channel regulation by calmodulin binding Saimi Y; Kung CFEBS Lett 1994[Aug]; 350 (2-3): 155-8While 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.|*Ion Channel Gating[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Calcium Channels/physiology[MESH]|Calmodulin/*physiology[MESH]|Drosophila melanogaster/physiology[MESH]|Molecular Sequence Data[MESH]|Muscle Proteins/physiology[MESH]|Muscles/physiology[MESH]|Paramecium/physiology[MESH]|Potassium Channels/physiology[MESH]|Ryanodine Receptor Calcium Release Channel[MESH]|Sensory Receptor Cells/physiology[MESH]|Smell/physiology[MESH]|Sodium Channels/physiology[MESH] |