ArticleProceedings of the National Academy of Sciences of the United States of America1994
Subunit 2 (or beta) of retinal rod cGMP-gated cation channel is a component of the 240-kDa channel-associated protein and mediates Ca(2+)-calmodulin modulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 170 citations in OpenAlex.
- Systematic functional evaluation of CNGA1 missense variants associated with retinitis pigmentosa.Molecular medicine (Cambridge, Mass.) · 2026Article
- Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin.International journal of molecular sciences · 2022Review
- Structural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel.Neuron · 2022Article
- The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods.Nature structural & molecular biology · 2022Article
- Structure of the human cone photoreceptor cyclic nucleotide-gated channel.Nature structural & molecular biology · 2022Article
- Cul3-Klhl18 ubiquitin ligase modulates rod transducin translocation during light-dark adaptation.The EMBO journal · 2019Article
- Inherited macular degeneration-associated mutations in CNGB3 increase the ligand sensitivity and spontaneous open probability of cone cyclic nucleotide-gated channels.Frontiers in physiology · 2015Article
- Calcium-calmodulin does not alter the anion permeability of the mouse TMEM16A calcium-activated chloride channel.The Journal of general physiology · 2014Article
- Cyclic nucleotide gated channels 7 and 8 are essential for male reproductive fertility.PloS one · 2013Article
- Article
- Age-related changes in Cngb1-X1 knockout mice: prolonged cone survival.Documenta ophthalmologica. Advances in ophthalmology · 2012Article
- Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of X-linked retinitis pigmentosa caused by mutations in RPGR.Advances in experimental medicine and biology · 2012Article
- Adaptation of mammalian photoreceptors to background light: putative role for direct modulation of phosphodiesterase.Molecular neurobiology · 2011Review
- Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels.Nature communications · 2011Article
- Article
- Calcium sets the physiological value of the dominant time constant of saturated mouse rod photoresponse recovery.PloS one · 2010Article
- Conformational rearrangements in the S6 domain and C-linker during gating in CNGA1 channels.European biophysics journal : EBJ · 2009Article
- Knockout of GARPs and the β-subunit of the rod cGMP-gated channel disrupts disk morphogenesis and rod outer segment structural integrity.Journal of cell science · 2009Article
- Movements of native C505 during channel gating in CNGA1 channels.European biophysics journal : EBJ · 2009Article
- How vision begins: an odyssey.Proceedings of the National Academy of Sciences of the United States of America · 2008Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cGMP-gated cation channel mediating visual transduction in retinal rods was recently found to comprise at least two subunits, 1 and 2 (or alpha and beta). SDS gels of the purified channel show, in addition to a 63-kDa protein band (subunit 1), a 240-kDa protein band that binds Ca(2+)-calmodulin, a modulator of the channel. To examine any connection between subunit 2 and the 240-kDa protein, cGMP-gated channels formed from the expressed cloned subunits in human embryonic kidney (HEK) 293 cells were tested for Ca(2+)-calmodulin effect. Homooligomeric channels formed by subunit 1 alone showed no sensitivity to Ca(2+)-calmodulin, and neither did heterooligomeric channels formed by subunit 1 and the short alternatively spliced form of subunit 2 (2a). By contrast, the cGMP half-activation constant (K1/2) for heterooligomeric channels formed from subunit 1 and the long form of subunit 2 (2b) was increased 1.5- to 2-fold by Ca(2+)-calmodulin, similar to the increase observed for the native channel. In Western blots of rod outer segment membranes, a subunit 2-specific antibody also recognized the 240-kDa protein. Finally, amino acid sequences derived from peptide fragments of the bovine 240-kDa protein showed approximately 80% identity to regions of subunit 2b of the human channel. These results together suggest that subunit 2b of the rod channel is a component of the 240-kDa protein and that it mediates the Ca(2+)-calmodulin modulation of the channel.
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