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

Haining Zhong, Laurie L. Molday, Robert S. Molday () and King-Wai Yau ()
Additional contact information
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

Nature, 2002, vol. 420, issue 6912, 193-198

Abstract: 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.

Date: 2002
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature01201 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:420:y:2002:i:6912:d:10.1038_nature01201

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature01201

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().