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The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry

Author

Listed:
  • Haining Zhong

    (Johns Hopkins University School of Medicine)

  • Laurie L. Molday

    (University of British Columbia)

  • Robert S. Molday

    (University of British Columbia)

  • King-Wai Yau

    (Johns Hopkins University School of Medicine
    Johns Hopkins University School of Medicine
    Johns Hopkins University School of Medicine)

Abstract

Cyclic nucleotide-gated (CNG) channels are crucial for visual and olfactory transductions1,2,3,4. These channels are tetramers and in their native forms are composed of A and B subunits5, with a stoichiometry thought to be 2A:2B (refs 6, 7). Here we report the identification of a leucine-zipper8-homology domain named CLZ (for carboxy-terminal leucine zipper). This domain is present in the distal C terminus of CNG channel A subunits but is absent from B subunits, and mediates an inter-subunit interaction. With cross-linking, non-denaturing gel electrophoresis and analytical centrifugation, this CLZ domain was found to mediate a trimeric interaction. In addition, a mutant cone CNG channel A subunit with its CLZ domain replaced by a generic trimeric leucine zipper produced channels that behaved much like the wild type, but less so if replaced by a dimeric or tetrameric leucine zipper. This A-subunit-only, trimeric interaction suggests that heteromeric CNG channels actually adopt a 3A:1B stoichiometry. Biochemical analysis of the purified bovine rod CNG channel confirmed this conclusion. This revised stoichiometry provides a new foundation for understanding the structure and function of the CNG channel family.

Suggested Citation

  • Haining Zhong & Laurie L. Molday & Robert S. Molday & King-Wai Yau, 2002. "The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry," Nature, Nature, vol. 420(6912), pages 193-198, November.
    • Handle: RePEc:nat:nature:v:420:y:2002:i:6912:d:10.1038_nature01201
    DOI: 10.1038/nature01201
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