PMID:12432397
| Citation |
Zhong, H, Molday, LL, Molday, RS and Yau, KW (2002) The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry. Nature 420:193-8 |
|---|---|
| Abstract |
Cyclic nucleotide-gated (CNG) channels are crucial for visual and olfactory transductions. These channels are tetramers and in their native forms are composed of A and B subunits, with a stoichiometry thought to be 2A:2B (refs 6, 7). Here we report the identification of a leucine-zipper-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. |
| Links |
PubMed PMC2877395 Online version:10.1038/nature01201 |
| Keywords |
Amino Acid Sequence; Animals; Cattle; Cell Line; Centrifugation; Chromatography, Gel; Cross-Linking Reagents; Cyclic Nucleotide-Gated Cation Channels; Humans; Ion Channels/chemistry; Ion Channels/genetics; Ion Channels/isolation & purification; Ion Channels/metabolism; Leucine Zippers/genetics; Mice; Molecular Sequence Data; Mutation; Precipitin Tests; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Rats; Retinal Rod Photoreceptor Cells; Structure-Activity Relationship |
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