Revisão Acesso aberto Revisado por pares

Ion channel regulation by calmodulin binding

1994; Wiley; Volume: 350; Issue: 2-3 Linguagem: Inglês

10.1016/0014-5793(94)00782-9

ISSN

1873-3468

Autores

Yoshiro Saimi, Ching Kung,

Tópico(s)

Physiological and biochemical adaptations

Resumo

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.

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