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Journal of Neuroscience, Vol 12, 3248-3256, Copyright © 1992 by Society for Neuroscience
Human rod photoreceptor cGMP-gated channel: amino acid sequence, gene structure, and functional expression
RS Dhallan, JP Macke, RL Eddy, TB Shows, RR Reed, KW Yau and J Nathans
Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Phototransduction in retinal rods involves a G-protein-mediated signaling
cascade that leads to cGMP hydrolysis and the closure of a cGMP-gated
channel. This channel has recently been purified from bovine retina and
molecularly cloned (Kaupp et al., 1989). We report here the cloning of cDNA
and genomic DNA encoding the human rod cGMP-gated channel, based upon its
homology to the bovine counterpart. The human mRNA structure differs from
the bovine in containing an Alu repetitive element spliced into the 5'
untranslated region. The human cGMP-gated channel gene (CNCG) is located on
chromosome 4 and contains at least 10 exons. One large exon encodes the
carboxy-terminal two-thirds of the protein, whereas seven small exons
encode the amino-terminal one-third of the protein. Alternative splicing
removes one of the small exons in a subset of transcripts in the human
retina, producing an internal in- frame deletion of 36 codons. When
expressed in a human embryonic kidney cell line (293S), the full-length
cDNA clone, but not the differentially spliced variant, produced functional
ion channels broadly similar to the native channels in vertebrate rods.
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