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Cyclic nucleotide-gated channel
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A cyclic nucleotide-gated (CNG) ion channel is any ion channel that opens in the presence of cyclic nucleotides.
Mechanism
The channels are gated by a chemical ligand (the cyclic nucleotide), but they are more similar in structure to the family of voltage-gated ion channels than to the ligand gated ones. In fact, the cyclic nucleotide-gated channels often have positively- or negatively-charged areas that may respond to changes in membrane potential. The purpose and function of these charged areas are not yet fully understood.
Functions
Cyclic nucleotide-gated channels are particularly important in several systems:
- In the visual system, a cGMP- (cyclic guanosine monophosphate-) gated channel is found in the outer membrane of retinal photoreceptor cells. In response to high levels of cGMP, the channels are open and allow positively-charged ions to flow into the cell, causing depolarization. This is the state of the cell in the dark (called the dark current), but a photon striking a photoreceptor in the cell causes a chain reaction that results in lower levels of cGMP and therefore hyperpolarization. Thus, these cells are actually more active in dark than in light.
Examples
Alpha
"Cyclic nucleotide gated channel alpha" subunits include
Beta-subunits include:
Hyperpolarization-activated
Other examples include the following "hyperpolarization-activated cyclic nucleotide-gated potassium channels" (HCN channels): HCN1, HCN2, HCN3, HCN4
References
- ^ Jenkins PM, Hurd TW, Zhang L, et al (2006). "Ciliary targeting of olfactory CNG channels requires the CNGB1b subunit and the kinesin-2 motor protein, KIF17". Curr. Biol. 16 (12): 1211–6. doi:10.1016/j.cub.2006.04.034. PMID 16782012.
- ^ DiFrancesco D (2006). "Serious workings of the funny current". Prog. Biophys. Mol. Biol. 90 (1-3): 13–25. doi:10.1016/j.pbiomolbio.2005.05.001. PMID 15975637.
- ^ a b c Walter F., PhD. Boron. Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. ISBN 1-4160-2328-3. Page 875
External links
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Membrane transport protein: ion channels |
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| Ca2+: Calcium channel |
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L-type/ Cavα ( 1.1, 1.2, 1.3, 1.4) • N-type/ Cavα2.2 • P-type/ Cavα( 2.1) • Q-type/ Cavα2.1 • R-type/ Cavα2.3 • T-type/ Cavα( 3.2)
α2δ-subunits ( 1, 2) • β-subunits ( β1, β2, β3, β4) • γ-subunits ( γ1, γ2, γ3, γ4)
Cation channels of sperm • Two-pore channel ( 1, 2)
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Ligand-gated
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| Na+: Sodium channel |
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Navα ( 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) • Navβ ( 1, 2, 3, 4)
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Other
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| K+: Potassium channel |
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Kvα (1-6) ( 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.10, 2.1, 2.2, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 4.3, 5.1, 6.1, 6.2, 6.3, 6.4)
Kvα (7-12) ( 7.1, 7.2, 7.3, 7.4, 7.5, 8.1, 8.2, 9.1, 9.2, 9.3, 10.1, 10.2, 11.1/hERG, 11.2, 11.3, 12.1, 12.2, 12.3)
Kvβ ( 1, 2, 3) • KCNIP ( 1, 2, 3, 4) • minK/ISK • MiRP ( 1, 2, 3) • Shaker gene
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Kir ( 1.1, 2.1, 2.2, 2.3, 2.4) • GIRK/ Kir ( 3.1, 3.2, 3.3, 3.4) • Kir ( 4.1, 4.2, 5.1, 6.1, 6.2, 7.1)
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K2P ( 1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)
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| M+: TRP cation channel |
TRPA ( 1) • TRPC ( 1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM ( 1, 2, 3, 4, 5, 6, 7, 8) • TRPML ( 1, 2, 3) • TRPP ( 1, 2) • TRPV ( 1, 2, 3, 4, 5, 6)
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| Cl-: Chloride channel |
CFTR • CLCA ( 1, 2, 3, 4) • CLCN ( 1, 2, 3, 4, 5, 6, 7, KA, KB) • CLIC ( 1, 2, 3, 4, 5, 6, L1) • CLNS ( 1A, 1B)
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| Cyclic nucleotide-gated |
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| Porin |
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| Other/general |
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