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Published November 25, 1994 | metadata_only
Journal Article

Calcium-Calmodulin Modulation of the Olfactory Cyclic Nucleotide-Gated Cation Channel


Although several ion channels have been reported to be directly modulated by calcium-calmodulin, they have not been conclusively shown to bind calmodulin, nor are the modulatory mechanisms understood. Study of the olfactory cyclic nucleotide-activated cation channel, which is modulated by calcium-calmodulin, indicates that calcium-calmodulin directly binds to a specific domain on the amino terminus of the channel. This binding reduces the effective affinity of the channel for cyclic nucleotides, apparently by acting on channel gating, which is tightly coupled to ligand binding. The data reveal a control mechanism that resembles those underlying the regulation of enzymes by calmodulin. The results also point to the amino-terminal part of the olfactory channel as an element for gating, which may have general significance in the operation of ion channels with similar overall structures.

Additional Information

© 1994 American Association for the Advancement of Science. 15 July 1994; Accepted 26 October 1994. We thank J. Finn, R.-C. Huang, R. L. Huganir, Y. Koutalos, J. Nathans, Y.-W. Peng, R. R. Reed, J. Schroeder, W.-P. Yu, and D. T.-C. Yue for discussions and comments; J. Finn for help with computer analysis and transfections; R. S. Dhallan for constructing some of the chimeras based on a method suggested by R. R. Reed; and G. Yellen for lending equipment and for first pointing out that the calcium-calmodulin-induced shift in ligand affinity of the olfactory channel may reflect a change in gating. Supported in part by NIH grant EY 06837.

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August 20, 2023
August 20, 2023