A new subunit of the cyclic nucleotide-gated cation channel in retinal rods

T. Y. Chen, Y. W. Peng, R. S. Dhallan, B. Ahamed, Randall R Reed, King-Wai Yau

Research output: Contribution to journalArticle

Abstract

Retinal rods respond to light with a membrane hyperpolarization produced by a G-protein-mediated signalling cascade that leads to cyclic GMP hydrolysis and the consequent closure of a cGMP-gated channel that is open in darkness1-7. A protein that forms this channel has recently been purified from bovine retinaH and molecularly cloned9, suggesting that the native cGMP-gated channel might be a homo-oligomer10. Here we report the cloning of another protein from human retina which has only about 30% overall identity to the rod channel subunit. This protein, immunocytochemically localized to rod outer segments, does not form functional channels by itself. However, when co-expressed with the cloned human rod channel protein11, it introduces rapid flickers to the channel openings that are characteristic of the native channel12-16. The hetero-oligomeric channel is also highly sensitive to the blocker L-cis-diltiazem, like the native channel15,17,18. This new protein thus seems to be another subunit of the native rod channel. The hetero-oligomeric nature of the rod channel means that it is no exception to a common motif shared by other ligand-gated channels.

Original languageEnglish (US)
Pages (from-to)764-767
Number of pages4
JournalNature
Volume362
Issue number6422
StatePublished - 1993

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Cyclic Nucleotide-Gated Cation Channels
Retinal Rod Photoreceptor Cells
Proteins
Ligand-Gated Ion Channels
Rod Cell Outer Segment
Diltiazem
Cyclic GMP
GTP-Binding Proteins
Retina
Organism Cloning
Hydrolysis
Light
Membranes

ASJC Scopus subject areas

  • General

Cite this

Chen, T. Y., Peng, Y. W., Dhallan, R. S., Ahamed, B., Reed, R. R., & Yau, K-W. (1993). A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. Nature, 362(6422), 764-767.

A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. / Chen, T. Y.; Peng, Y. W.; Dhallan, R. S.; Ahamed, B.; Reed, Randall R; Yau, King-Wai.

In: Nature, Vol. 362, No. 6422, 1993, p. 764-767.

Research output: Contribution to journalArticle

Chen, TY, Peng, YW, Dhallan, RS, Ahamed, B, Reed, RR & Yau, K-W 1993, 'A new subunit of the cyclic nucleotide-gated cation channel in retinal rods', Nature, vol. 362, no. 6422, pp. 764-767.
Chen TY, Peng YW, Dhallan RS, Ahamed B, Reed RR, Yau K-W. A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. Nature. 1993;362(6422):764-767.
Chen, T. Y. ; Peng, Y. W. ; Dhallan, R. S. ; Ahamed, B. ; Reed, Randall R ; Yau, King-Wai. / A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. In: Nature. 1993 ; Vol. 362, No. 6422. pp. 764-767.
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AB - Retinal rods respond to light with a membrane hyperpolarization produced by a G-protein-mediated signalling cascade that leads to cyclic GMP hydrolysis and the consequent closure of a cGMP-gated channel that is open in darkness1-7. A protein that forms this channel has recently been purified from bovine retinaH and molecularly cloned9, suggesting that the native cGMP-gated channel might be a homo-oligomer10. Here we report the cloning of another protein from human retina which has only about 30% overall identity to the rod channel subunit. This protein, immunocytochemically localized to rod outer segments, does not form functional channels by itself. However, when co-expressed with the cloned human rod channel protein11, it introduces rapid flickers to the channel openings that are characteristic of the native channel12-16. The hetero-oligomeric channel is also highly sensitive to the blocker L-cis-diltiazem, like the native channel15,17,18. This new protein thus seems to be another subunit of the native rod channel. The hetero-oligomeric nature of the rod channel means that it is no exception to a common motif shared by other ligand-gated channels.

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