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Ion channel regulation by calmodulin binding
Author(s) -
Saimi Yoshiro,
Kung Ching
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00782-9
Subject(s) - calmodulin , ion channel , paramecium , microbiology and biotechnology , biology , biophysics , chemistry , biochemistry , receptor , enzyme
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.