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Rotational movement during cyclic nucleotide-gated channel opening

Author

Listed:
  • J. P. Johnson

    (Box 357290, University of Washington School of Medicine)

  • William N. Zagotta

    (Box 357290, University of Washington School of Medicine)

Abstract

Cyclic nucleotide-gated (CNG) channels are crucial components of visual, olfactory and gustatory signalling pathways. They open in response to direct binding of intracellular cyclic nucleotides and thus contribute to cellular control of both the membrane potential and intracellular Ca2+ levels1. Cytosolic Ni2+ potentiates the rod channel (CNG1) response to cyclic nucleotides2,3,4 and inhibits the olfactory channel (CNG2) response5. Modulation is due to coordination of Ni2+ by channel-specific histidines in the C-linker, between the S6 transmembrane segment and the cyclic nucleotide-binding domain. Here we report, using a histidine scan of the initial C-linker of the CNG1 channel, stripes of sites producing Ni2+ potentiation or Ni2+ inhibition, separated by 50° on an α-helix. These results suggest a model for channel gating where rotation of the post-S6 region around the channel's central axis realigns the Ni2+-coordinating residues of multiple subunits. This rotation probably initiates movement of the S6 and pore opening.

Suggested Citation

  • J. P. Johnson & William N. Zagotta, 2001. "Rotational movement during cyclic nucleotide-gated channel opening," Nature, Nature, vol. 412(6850), pages 917-921, August.
    • Handle: RePEc:nat:nature:v:412:y:2001:i:6850:d:10.1038_35091089
    DOI: 10.1038/35091089
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    Cited by:

    1. Johansen B. Amin & Miaomiao He & Ramesh Prasad & Xiaoling Leng & Huan-Xiang Zhou & Lonnie P. Wollmuth, 2023. "Two gates mediate NMDA receptor activity and are under subunit-specific regulation," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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