Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels

Noah G. Shuart, Yoni Haitin, Stacey S. Camp, Kevin D. Black and William N. Zagotta ()
Additional contact information
Noah G. Shuart: University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA.
Yoni Haitin: University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA.
Stacey S. Camp: University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA.
Kevin D. Black: University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA.
William N. Zagotta: University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA.

Nature Communications, 2011, vol. 2, issue 1, 1-10

Abstract: Abstract Molecular determinants of ion channel tetramerization are well characterized, but those involved in heteromeric channel assembly are less clearly understood. The heteromeric composition of native channels is often precisely controlled. Cyclic nucleotide-gated (CNG) channels from rod photoreceptors exhibit a 3:1 stoichiometry of CNGA1 and CNGB1 subunits that tunes the channels for their specialized role in phototransduction. Here we show, using electrophysiology, fluorescence, biochemistry, and X-ray crystallography, that the mechanism for this controlled assembly is the formation of a parallel 3-helix coiled-coil domain of the carboxy-terminal leucine zipper region of CNGA1 subunits, constraining the channel to contain three CNGA1 subunits, followed by preferential incorporation of a single CNGB1 subunit. Deletion of the carboxy-terminal leucine zipper domain relaxed the constraint and permitted multiple CNGB1 subunits in the channel. The X-ray crystal structures of the parallel 3-helix coiled-coil domains of CNGA1 and CNGA3 subunits were similar, suggesting that a similar mechanism controls the stoichiometry of cone CNG channels.

Date: 2011
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms1466 Abstract (text/html)

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:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1466

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

DOI: 10.1038/ncomms1466

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

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