Ankyrin-G promotes cyclic nucleotide-gated channel transport to rod photoreceptor sensory cilia.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 19299621.
- Also identified by DOI 10.1126/science.1169789 and PMC identifier 2792576.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Cyclic nucleotide-gated (CNG) channels localize exclusively to the plasma membrane of photosensitive outer segments of rod photoreceptors where they generate the electrical response to light. Here, we report the finding that targeting of CNG channels to the rod outer segment required their interaction with ankyrin-G. Ankyrin-G localized exclusively to rod outer segments, coimmunoprecipitated with the CNG channel, and bound to the C-terminal domain of the channel beta1 subunit. Ankyrin-G depletion in neonatal mouse retinas markedly reduced CNG channel expression. Transgenic expression of CNG channel beta-subunit mutants in Xenopus rods showed that ankyrin-G binding was necessary and sufficient for targeting of the beta1 subunit to outer segments. Thus, ankyrin-G is required for transport of CNG channels to the plasma membrane of rod outer segments.
Medical subject headings
- Ankyrins
- Cilia
- Cyclic Nucleotide-Gated Cation Channels
- Rod Cell Outer Segment