Relevant bibliographies by topics / Cyclic nucleotide-gated channel

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Academic literature on the topic 'Cyclic nucleotide-gated channel'

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Published: 14 March 2023

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Journal articles on the topic "Cyclic nucleotide-gated channel"

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Kaupp, U. Benjamin, and Reinhard Seifert. "Cyclic Nucleotide-Gated Ion Channels." Physiological Reviews 82, no. 3 (January 7, 2002): 769–824. http://dx.doi.org/10.1152/physrev.00008.2002.

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Cyclic nucleotide-gated (CNG) channels are nonselective cation channels first identified in retinal photoreceptors and olfactory sensory neurons (OSNs). They are opened by the direct binding of cyclic nucleotides, cAMP and cGMP. Although their activity shows very little voltage dependence, CNG channels belong to the superfamily of voltage-gated ion channels. Like their cousins the voltage-gated K+ channels, CNG channels form heterotetrameric complexes consisting of two or three different types of subunits. Six different genes encoding CNG channels, four A subunits (A1 to A4) and two B subunits (B1 and B3), give rise to three different channels in rod and cone photoreceptors and in OSNs. Important functional features of these channels, i.e., ligand sensitivity and selectivity, ion permeation, and gating, are determined by the subunit composition of the respective channel complex. The function of CNG channels has been firmly established in retinal photoreceptors and in OSNs. Studies on their presence in other sensory and nonsensory cells have produced mixed results, and their purported roles in neuronal pathfinding or synaptic plasticity are not as well understood as their role in sensory neurons. Similarly, the function of invertebrate homologs found in Caenorhabditis elegans, Drosophila,and Limulus is largely unknown, except for two subunits of C. elegans that play a role in chemosensation. CNG channels are nonselective cation channels that do not discriminate well between alkali ions and even pass divalent cations, in particular Ca2+. Ca2+ entry through CNG channels is important for both excitation and adaptation of sensory cells. CNG channel activity is modulated by Ca2+/calmodulin and by phosphorylation. Other factors may also be involved in channel regulation. Mutations in CNG channel genes give rise to retinal degeneration and color blindness. In particular, mutations in the A and B subunits of the CNG channel expressed in human cones cause various forms of complete and incomplete achromatopsia.
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James, Zachary M., and William N. Zagotta. "Structural insights into the mechanisms of CNBD channel function." Journal of General Physiology 150, no. 2 (December 12, 2017): 225–44. http://dx.doi.org/10.1085/jgp.201711898.

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Cyclic nucleotide-binding domain (CNBD) channels are a family of ion channels in the voltage-gated K+ channel superfamily that play crucial roles in many physiological processes. CNBD channels are structurally similar but functionally very diverse. This family includes three subfamilies: (1) the cyclic nucleotide-gated (CNG) channels, which are cation-nonselective, voltage-independent, and cyclic nucleotide-gated; (2) the hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which are weakly K+ selective, hyperpolarization-activated, and cyclic nucleotide-gated; and (3) the ether-à-go-go-type (KCNH) channels, which are strongly K+ selective, depolarization-activated, and cyclic nucleotide-independent. Recently, several high-resolution structures have been reported for intact CNBD channels, providing a structural framework to better understand their diverse function. In this review, we compare and contrast the recent structures and discuss how they inform our understanding of ion selectivity, voltage-dependent gating, and cyclic nucleotide–dependent gating within this channel family.
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Becchetti, Andrea, Katia Gamel, and Vincent Torre. "Cyclic Nucleotide–Gated Channels." Journal of General Physiology 114, no. 3 (September 1, 1999): 377–92. http://dx.doi.org/10.1085/jgp.114.3.377.

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In voltage- and cyclic nucleotide–gated ion channels, the amino-acid loop that connects the S5 and S6 transmembrane domains, is a major component of the channel pore. It determines ion selectivity and participates in gating. In the α subunit of cyclic nucleotide–gated channels from bovine rod, the pore loop is formed by the residues R345–S371, here called R1-S27. These 24 residues were mutated one by one into a cysteine. Mutant channels were expressed in Xenopus laevis oocytes and currents were recorded from excised membrane patches. The accessibility of the substituted cysteines from both sides of the plasma membrane was tested with the thiol-specific reagents 2-aminoethyl methanethiosulfonate (MTSEA) and [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET). Residues V4C, T20C, and P22C were accessible to MTSET only from the external side of the plasma membrane, and to MTSEA from both sides of the plasma membrane. The effect of MTSEA applied to the inner side of T20C and P22C was prevented by adding 10 mM cysteine to the external side of the plasma membrane. W9C was accessible to MTSET from the internal side only. L7C residue was accessible to internal MTSET, but the inhibition was partial, ∼50% when the MTS compound was applied in the absence of cGMP and 25% when it was applied in the presence of cGMP, suggesting that this residue is not located inside the pore lumen and that it changes its position during gating. Currents from T15C and T16C mutants were rapidly potentiated by intracellular MTSET. In T16C, a slower partial inhibition took place after the initial potentiation. Current from I17C progressively decayed in inside-out patches. The rundown was accelerated by inwardly applied MTSET. The accessibility results of MTSET indicate a well-defined topology of the channel pore in which residues between L7 and I17 are inwardly accessible, residue G18 and E19 form the narrowest section of the pore, and T20, P21, P22 and V4 are outwardly accessible.
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Santy, Lorraine C., and Guido Guidotti. "Expression of a single gene produces both forms of skeletal muscle cyclic nucleotide-gated channels." American Journal of Physiology-Endocrinology and Metabolism 273, no. 6 (December 1, 1997): E1140—E1148. http://dx.doi.org/10.1152/ajpendo.1997.273.6.e1140.

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Cyclic nucleotide-gated cation channels in skeletal muscle are responsible for insulin-activated sodium entry into this tissue (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267: 832–841, 1992). These channels have previously been isolated from rabbit skeletal muscle by 8-bromoguanosine 3′,5′-cyclic monophosphate (8-BrcGMP) affinity chromatography, which separates them into two populations differing in nucleotide affinity [L. C. Santy and G. Guidotti. Am. J. Physiol. 271 ( Endocrinol. Metab. 34): E1051-E1060, 1996]. In this study, a polymerase chain reaction approach was used to identify skeletal muscle cyclic nucleotide-gated channel cDNAs. Rabbit skeletal muscle expresses the same cyclic nucleotide-gated channel as rabbit aorta (M. Biel, W. Altenhofen, R. Hullin, J. Ludwig, M. Freichel, V. Flockerzi, N. Dascal, U. B. Kaupp, and F. Hofmann. FEBS Lett. 329: 134–138, 1993). The entire cDNA for this gene was cloned from rabbit skeletal muscle and an antiserum to this protein produced. Expression of this cDNA produces a 63-kDa protein with cyclic nucleotide-gated channel activity. A similarly sized immunoreactive protein is present in sarcolemma. Purification of the expressed channels reveals that this single gene produces both native skeletal muscle channel populations.
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Bej, Aritra, and James B. Ames. "Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin." International Journal of Molecular Sciences 23, no. 22 (November 16, 2022): 14143. http://dx.doi.org/10.3390/ijms232214143.

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Retinal cyclic nucleotide-gated (CNG) ion channels bind to intracellular cGMP and mediate visual phototransduction in photoreceptor rod and cone cells. Retinal rod CNG channels form hetero-tetramers comprised of three CNGA1 and one CNGB1 protein subunits. Cone CNG channels are similar tetramers consisting of three CNGA3 and one CNGB3 subunits. Calmodulin (CaM) binds to two distinct sites (CaM1: residues 565–587 and CaM2: residues 1120–1147) within the cytosolic domains of rod CNGB1. The binding of Ca2+-bound CaM to CNGB1 promotes the Ca2+-induced desensitization of CNG channels in retinal rods that may be important for photoreceptor light adaptation. Mutations that affect Ca2+-dependent CNG channel function are responsible for inherited forms of blindness. In this review, we propose structural models of the rod CNG channel bound to CaM that suggest how CaM might cause channel desensitization and how dysregulation of the channel may lead to retinal disease.
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Fodor, Anthony A., Sharona E. Gordon, and William N. Zagotta. "Mechanism of Tetracaine Block of Cyclic Nucleotide-gated Channels." Journal of General Physiology 109, no. 1 (January 1, 1997): 3–14. http://dx.doi.org/10.1085/jgp.109.1.3.

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Local anesthetics are a diverse group of ion channel blockers that can be used to probe conformational changes in the pore. We examined the effects of the local anesthetic tetracaine on rod and olfactory cyclic nucleotide-gated channels expressed from subunit 1 in Xenopus oocytes. We found that 40 μM tetracaine effectively blocked the bovine rod channel but not the rat olfactory channel at saturating concentrations of cGMP. By testing chimeric channels containing regions of sequence from both rod and olfactory channels, we found that determinants of apparent affinity for tetracaine at saturating cGMP did not map to any one region of the channel sequence. Rather, the differences in apparent affinity could be explained by differences between the chimeras in the free energy of the opening allosteric transition. If a channel construct (such as the rod channel) spent appreciable time in the closed state at saturating cGMP, then it had a high apparent affinity for tetracaine. If, on the other hand, a channel construct (such as the olfactory channel) spent little time in the closed state at saturating cGMP, then it had a low apparent affinity for tetracaine. Furthermore, tetracaine became more effective at low concentrations of cGMP and at saturating concentrations of cAMP, conditions which permit the channels to spend more time in the closed configuration. These results were well fit by a model in which tetracaine binds more tightly to the closed channel than to the open channel. Dose-response curves for tetracaine in the presence of saturating cGMP are well fit with a Michaelis-Menten binding scheme Indicating that a single tetracaine molecule is sufficient to produce block. In addition, tetracaine block is voltage dependent with an effective zδ of +0.56. These data are consistent with a pore-block hypothesis. The finding that tetracaine is a state-dependent pore blocker suggests that the inner mouth of the pore of cyclic nucleotide-gated channels undergoes a conformational change during channel opening.
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James, Zachary M., Andrew J. Borst, Yoni Haitin, Brandon Frenz, Frank DiMaio, William N. Zagotta, and David Veesler. "CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel." Proceedings of the National Academy of Sciences 114, no. 17 (April 10, 2017): 4430–35. http://dx.doi.org/10.1073/pnas.1700248114.

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Cyclic nucleotide-gated (CNG) and hyperpolarization-activated cyclic nucleotide-regulated (HCN) ion channels play crucial physiological roles in phototransduction, olfaction, and cardiac pace making. These channels are characterized by the presence of a carboxyl-terminal cyclic nucleotide-binding domain (CNBD) that connects to the channel pore via a C-linker domain. Although cyclic nucleotide binding has been shown to promote CNG and HCN channel opening, the precise mechanism underlying gating remains poorly understood. Here we used cryoEM to determine the structure of the intact LliK CNG channel isolated from Leptospira licerasiae—which shares sequence similarity to eukaryotic CNG and HCN channels—in the presence of a saturating concentration of cAMP. A short S4–S5 linker connects nearby voltage-sensing and pore domains to produce a non–domain-swapped transmembrane architecture, which appears to be a hallmark of this channel family. We also observe major conformational changes of the LliK C-linkers and CNBDs relative to the crystal structures of isolated C-linker/CNBD fragments and the cryoEM structures of related CNG, HCN, and KCNH channels. The conformation of our LliK structure may represent a functional state of this channel family not captured in previous studies.
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Santy, L. C., and G. Guidotti. "Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 271, no. 6 (December 1, 1996): E1051—E1060. http://dx.doi.org/10.1152/ajpendo.1996.271.6.e1051.

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A cyclic nucleotide-gated channel present in skeletal muscle plasma membrane has previously been identified as being responsible for insulin-activated sodium entry into muscle cells (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267:832-841, 1992). We have isolated this channel activity to further study and characterize it. The channel was solubilized from rabbit skeletal muscle sarcolemma and functionally reconstituted into phospholipid vesicles, as assayed by patch-clamp analysis of the reconstituted proteins. Channel activity was isolated by 8-bromo-guanosine 3',5'-cyclic monophosphate affinity chromatography, producing two distinct peaks of cyclic nucleotide-gated channel activity. These two types of channel activity differ in guanosine 3',5'-cyclic monophosphate affinity and in the ability to be opened by adenosine 3',5'-cyclic monophosphate. The cyclic nucleotide-gated channel from rod outer segments also forms two peaks of activity when purified in this manner. The presence of two forms of channel activity could have implications for the mechanism of insulin-activated sodium entry.
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Paoletti, Pierre, Edgar C. Young, and Steven A. Siegelbaum. "C-Linker of Cyclic Nucleotide–gated Channels Controls Coupling of Ligand Binding to Channel Gating." Journal of General Physiology 113, no. 1 (January 1, 1999): 17–34. http://dx.doi.org/10.1085/jgp.113.1.17.

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Cyclic nucleotide–gated channels are composed of a core transmembrane domain, structurally homologous to the voltage-gated K+ channels, and a cytoplasmic ligand-binding domain. These two modules are joined by ∼90 conserved amino acids, the C-linker, whose precise role in the mechanism of channel activation by cyclic nucleotides is poorly understood. We examined cyclic nucleotide–gated channels from bovine photoreceptors and Caenorhabditis elegans sensory neurons that show marked differences in cyclic nucleotide efficacy and sensitivity. By constructing chimeras from these two channels, we identified a region of 30 amino acids in the C-linker (the L2 region) as an important determinant of activation properties. An increase in both the efficacy of gating and apparent affinity for cGMP and cAMP can be conferred onto the photoreceptor channel by the replacement of its L2 region with that of the C. elegans channel. Three residues within this region largely account for this effect. Despite the profound effect of the C-linker region on ligand gating, the identity of the C-linker does not affect the spontaneous, ligand-independent open probability. Based on a cyclic allosteric model of activation, we propose that the C-linker couples the opening reaction in the transmembrane core region to the enhancement of the affinity of the open channel for agonist, which underlies ligand gating.
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Gerhardt, Maximilian J., Siegfried G. Priglinger, Martin Biel, and Stylianos Michalakis. "Biology, Pathobiology and Gene Therapy of CNG Channel-Related Retinopathies." Biomedicines 11, no. 2 (January 19, 2023): 269. http://dx.doi.org/10.3390/biomedicines11020269.

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The visual process begins with the absorption of photons by photopigments of cone and rod photoreceptors in the retina. In this process, the signal is first amplified by a cyclic guanosine monophosphate (cGMP)-based signaling cascade and then converted into an electrical signal by cyclic nucleotide-gated (CNG) channels. CNG channels are purely ligand-gated channels whose activity can be controlled by cGMP, which induces a depolarizing Na+/Ca2+ current upon binding to the channel. Structurally, CNG channels belong to the superfamily of pore-loop cation channels and share structural similarities with hyperpolarization-activated cyclic nucleotide (HCN) and voltage-gated potassium (KCN) channels. Cone and rod photoreceptors express distinct CNG channels encoded by homologous genes. Mutations in the genes encoding the rod CNG channel (CNGA1 and CNGB1) result in retinitis-pigmentosa-type blindness. Mutations in the genes encoding the cone CNG channel (CNGA3 and CNGB3) lead to achromatopsia. Here, we review the molecular properties of CNG channels and describe their physiological and pathophysiological roles in the retina. Moreover, we summarize recent activities in the field of gene therapy aimed at developing the first gene therapies for CNG channelopathies.
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Dissertations / Theses on the topic "Cyclic nucleotide-gated channel"

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Cukkemane, Abhishek. "Structural and functional studies of a prokaryotic cyclic nucleotide gated channel /." Jülich : Forschungszentrum, Zentralbibliothek, 2008. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=016779692&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Sunderman, Elizabeth R. "Single-channel kinetic analysis of the allosteric transition of rod cyclic nucleotide-gated channels /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/10526.

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Matulef, Kimberly Irene. "Cysteine-scanning mutagenesis of the ligand-binding domain of cyclic nucleotide-gated channels /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/5032.

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Lolicato, M. G. L. "STRUCTURAL STUDIES ON THE REGULATORY DOMAIN OF THREE HCN (HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED) CHANNEL ISOFORMS." Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/168356.

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Hyperpolarization-activated cyclic nucleotide gated (HCN) chan- nels underlie the If /Ih cation currents that control pacemaker activity in heart and brain. HCN channels are dually ac- tivated by membrane hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD). Binding of cAMP shifts the activation curve of HCN2 and HCN4 by 17 mV, but that of HCN1 by only 2-4 mV. Tetramerization of the CNBD is seemingly part of the cAMP-induced allosteric con- formational changes that increase the open probability of the channel pore. We have obtained the crystal structures of the CNBD of the three isoforms, but the analysis revealed a very conserved structure between HCN1 versus HCN2 and HCN4, except for a loop of β-roll, previously shown to regulate the binding affinity of HCN4. We measured the binding affin- ity of the CNBD for the cAMP and the different propensity of the regulatory domain to tetramerize in absence or presence of the ligand. We confirm that tetramerization is the primary ef- fect of cAMP binding, and the first step in the transmission of this signal, that eventually removes the inhibition imposed by the CNBD on the channel. Accordingly, cAMP- binding releases HCN2 and HCN4 from inhibition, but has little or no effect on HCN1. Our data demonstrate that in HCN1 the CNBD is already tetrameric at basal cAMP concentrations contrary to HCN2 and HCN4. HCN1 shows this peculiar behavior despite its cAMP- binding affinity is in the same range of the affinity found in HCN2 and HCN4. This can be explained by two different 3 affinity states (high and low). HCN1 is, at low cAMP concen- trations, already switched to the low affinity conformation, while the high affinity state is not measurable because the binding site is already occupied. Our results offer a logical explanation for the behavior of HCN1 and an experimental support to the leading hypothesis that ligand-induced tetramerization removes tonic inhibition from the pore. In addition, some more inter- esting information arose from the crystal structure, highlighting an additional electron density close to the tetramerization inter- face of the proteins. We investigated a range of molecules that could bind the proteins in that pocket and potentially alter the functionality of the channel.
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Becirovic, Elvir. "Role of the CNGB1a Subunit of the Rod Cyclic Nucleotide-Gated Channel in Channel Gating and Pathogenesis of Retinitis Pigmentosa." Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-119088.

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Tanaka, Naoto. "A MISSENSE MUTATION IN CONE PHOTORECEPTOR CYCLIC NUCLEOTIDE-GATED CHANNELS ASSOCIATED WITH CANINE DAYLIGHT BLINDNESS OFFERS INSIGHT INTO CHANNEL STRUCTURE AND FUNCTION." Diss., Temple University Libraries, 2013. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/246634.

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Biology
Ph.D.
Cone cyclic nucleotide-gated (CNG) channels are located in the retinal outer segments, mediating daylight color vision. The channel is a tetramer of A-type (CNGA3) and B-type (CNGB3) subunits. CNGA3 subunits are able to form homotetrameric channels, but CNGB3 exhibits channel function only when co-expressed with CNGA3. Mutations in the genes encoding these cone CNG subunits are associated with achromatopsia, an autosomal recessive genetic disorder which causes incomplete or complete loss of daylight and color vision. A missense mutation, aspartatic acid (Asp) to asparagine (Asn) at position 262 in the canine CNGB3 subunit (cB3-D262N), results in loss of cone function and therefore daylight blindness, highlighting the crucial role of this aspartic acid residue for proper channel biogenesis and/or function. Asp 262 is located in a conserved region of the second transmembrane segment containing three Asp residues designated the Tri-Asp motif. We exploit the conservation of these residues in CNGA3 subunits to examine the motif using a combination of experimental and computational approaches. Mutations of these conserved Asp residues result in a loss of nucleotide-activated currents and mislocalization in heterologous expression. Co-expressing CNGB3 Tri-Asp mutants with wild type CNGA3 results in functional channels, however, their electrophysiological characterization matches the properties of homomeric CNGA3 tetramers. This failure to record heteromeric currents implies that Asp/Asn mutations impact negatively both CNGA3 and CNGB3 subunits. A homology model of canine CNGA3 relaxed in a membrane using molecular dynamics simulations suggests that the Tri-Asp motif is involved in non-specific salt bridge pairings with positive residues of S3 - S4. We propose that the CNGB3-D262N mutation in daylight blind dogs results in the loss of these interactions and leads to an alteration of the electrostatic equilibrium in the S1 - S4 bundle. Because residues analogous to Tri-Asp residues in the voltage-gated Shaker K+ channel superfamily were implicated in monomer folding, we hypothesize that destabilizing these electrostatic interactions might impair the monomer folding state in D262N mutant CNG channels during biogenesis. Another missesnse sense mutation, Arginine (Arg) to tryptophan (Trp) at position 424 in the canine CNGA3 subunit (cA3-R424W), also results in loss of cone function. An amino acid sequence alignment with Shaker K+ channel superfamily indicates that this R424 residue is located in the C-terminal end of the sixth transmembrane segment. A3-R424W mutant channels resulted in no cyclic nucleotide-activated currents and mislocalization with intracellular aggregates. However, the localization of cA3-R424W mutant channels was not affected as severely as the Asp/Asn mutation in S2 Tri-Asp motif, showing a lot of cells with the proper localization of Golgi-like and membrane fluorescence. Moreover, the substitution of Arg 424 to Lysine (Lys), conserving the positive charge, preserved channel function in some cells, which is different from the results of the S2 Tri-Asp motif in which the Asp/Glu substitutions, conserving the negative charge, leads to loss of cyclic nucleotide-activated currents. Even though these missense mutations are both associated with canine daylight blindness, the Arg 424 residue might not be as critical for folding as the Tri-Asp residues in the S2 Tri-Asp motif and might be more of a problem in channel structure and function. The cA3 model relaxed with MD simulations indicated a possible interaction of Arg 424 with the Glu 304 residue in the S4-S5 linker. This hypothesis is supported by electrophysiological data in which the double mutation of reversing these residues, Glu 306 to Arg and Arg 424 to Glu (E306R-R424E) preserves channel function. In the model, this salt bridge appears to contribute to stabilization of the open pore state. The R424W mutation might disrupt the salt bridge formation, leading to deforming and closing the pore region.
Temple University--Theses
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Schünke, Sven Verfasser], Dieter [Akademischer Betreuer] [Willbold, and Lutz [Akademischer Betreuer] Schmitt. "NMR solution structures of the MloK1 cyclic nucleotide-gated ion channel binding domain / Sven Schünke. Gutachter: Lutz Schmitt. Betreuer: Dieter Willbold." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2011. http://d-nb.info/1015434975/34.

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Hundal, Sukhinder Paul Singh. "Molecular cloning, characterisation and function expression of cyclic nucleotide-gated ion channel genes expressed in sino-atrial node region of heart." Thesis, University of Leicester, 1994. http://hdl.handle.net/2381/35257.

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Pacemaker cells of the mammalian sino-atrial node (SAN) contain a hyperpolarization-activated, non-specific cationic current, If which is an important component involved in the initiation and neurotransmitter-mediated control of cardiac rhythm. cAMP can directly modulate If by a mechanism independent of phosphorylation, demonstrating that cyclic nucleotide-sensitive ion channel genes are expressed within cardiac pacemaker cells. Through a combination of library screening methods based on cross-hybridising cyclic nucleotide-gated channel probes and a PCR 'fingerprint' employing primers designed to sequences encoding an ion channel cyclic nucleotide-binding domain, partial cDNA clones were isolated from a prepared sino-atrial node regional-specific cDNA library, which were either homologues of previously identified ion channels shown to be expressed in sensory tissues or putative new channel clones. Isolate rscNGC 1 following retrieval of a full coding region by anchor-PCR, demonstrated 90.4% sequence identity to the a-subunit of the rod photoreceptor cGMP-gated channel. The PCR 'fingerprint' identified a SAN homologue of the olfactory neuron cAMP-gated channel within library aliquots. This was the first demonstration that two distinct cyclic nucleotide-gated ion channel genes were expressed in SAN region of heart. Heterologous expression of rscNGC 1 following micro-injection of capped cRNA in Xenopus oocytes, gave rise to cGMP-stimulated channel activity exhibiting electrophysiological properties similar to the characterised a-subunit of the rod photoreceptor cGMP-gated channel. A reconstituted second messenger-pathway mediating endogenous receptor coupling to heterologously expressed cAMP-gated ion channels - shown to be present within native nodal tissue - was attempted within MEL cells. However, the absence of endogenous receptors positively-coupled to adenylyl cyclase within MEL cells, and the inability to functional characterise cAMP-stimulated cationic conductances via electrophysiological methods, prevented such studies. Thus demonstrating the inappropriateness of the MEL cell, as a heterologous system for studying receptor-mediated second messenger coupling to cNG channels. Although cyclic nucleotide-gated ion channels are obligatorily coupled to intracellular signalling agonists commonly found in heart, they have yet to be described in functional terms within SAN or any other cardiac subregion. It is postulated that they may have a role in vasculature - underlying mechanisms of smooth muscle relaxation.
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Kimura, Koji. "Hyperpolarization-activated, cyclic nucleotide-gated HCN2 cation channel forms a protein assembly with multiple neuronal scaffold proteins in distinct modes of protein-protein interaction." Kyoto University, 2004. http://hdl.handle.net/2433/145287.

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Arrigoni, C. "MODULATION OF PORE GATING BY ¿SENSOR¿ DOMAINS IN VOLTAGE-GATED K+ CHANNELS." Doctoral thesis, Università degli Studi di Milano, 2013. http://hdl.handle.net/2434/215591.

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Many proteins in nature show a modular topology, because it is possible to recognize functional modules responsible of distinguishable functions in the protein. Voltage-gated can be considered modular proteins. The superfamily of voltage-gated channels is composed of channels in which a pore-module is in charge of generating an ion conductance across the cell membrane, and other “sensor”-modules perceive different stimuli and transmit them to the pore, readjusting the conductance in response to changes within the cell. The sensor module in voltage-gated channels is the voltage sensing domain. It is composed of four transmembrane segments and it is able to feel the electrical properties of the membrane, such as changes in potential and, through a mechanical load applied by a short linker, to affect the gating of the pore (i.e. opening or closure of the channel). A more sophisticated regulation is possible thanks to other modules fused to the same channel. Ligand-gated channels usually exhibit a C-terminal domain exposed in the cytoplasm, in contact with all the variable concentration of second messengers, able to modulate the activity of the channel. In this group, cyclic nucleotide-gated channels have a C-terminal domain, composed of a binding domain (CNBD) that respond to difference in concentration of cAMP or cGMP, and a C-linker region, connecting the CNBD to the pore. The CNBD acts as an allosteric domain, and modulate the channel opening upon cAMP binding.The idea that these domains evolved independently before fusing in a single protein, is strengthened by the fact that similar domains are found in a large variety of proteins, that don’t belong to channels family. For example, recently, a new enzyme was discovered, the voltage-sensing phosphatase (VSP) of Ciona intestinalis, whose voltage-sensor domain is fused to a phosphatase. The CNBD of the hyperpolarized cyclic nucleotide-activated channels (HCN), has a conserved structure compared to that of the cAMP-dependent protein kinases. My PhD thesis addresses two different topics, but in both cases I investigated how sensor-modules can give a sophisticated regulation of channel gating. In the first part, I approached the problem about how voltage-dependence originated in voltage-gated channels, in particular I obtained a voltage-gated K + channel fusing two unrelated protein modules: the voltage sensing domain of Ci-VSP and the pore-channel PBCV-1 Kcv. The fusion between a voltage sensor and a potassium channel with a quasi-ohmic behaviour generates a chimaeric protein called KvSynth1, an delayed outward rectifier potassium channel. KvSynth1 retains the pore properties of Kcv (selectivity and filter gating) and the voltage dependence of the Ci-VSP (half activation potential, slope factor, shift of activation curve due to mutations). Moreover, the quality of the rectification is dependent on the length of the linker between the two modules. This highlights a mechanic role of the linker in transmitting the movement of the sensor to the pore, and shows that electromechanical coupling can occur without co-evolution of the two domains. In the second part, the allosteric modulation of the cyclic nucleotide binding domain of HCN channels has been studied on the basis of our findings in the crystal structure of the CNBD of the isoform 4 of HCN (hyperpolarized cyclic nucleotide-activated) channels. HCN are the molecular determinant of the If current, responsible of the autonomic regulation of the heart. In the structure of HCN4 CNBD a putative binding site for cyclic nucleotides in the C-linker region was found. Occupancy of this binding site by the prokaryote second messenger c-di-GMP can completely revert the effect of cAMP in the micromolar range. Docking a large set of molecules in the binding pocket, another compound was identified, (N’-biphenyl-2-yl-N-[1-(3-cyanobenzyl)piperidin-4-yl]-N-(pyridin-3-ylmethyl)urea), able to give the same effect on cAMP modulation. The effect of these molecules is restricted to HCN4; this isoform selectivity underlies that, although the C-terminus of the three isoforms is structured in a similar way, the modulation can be different. Some different features of HCN1, HCN2 and HCN4 were already analysed previously. These results highlight the presence of an second modulatory pathway in HCN channels, indicate a potential drug binding site for heart rate modulation and advance understanding of the mechanism of efficacy of cAMP binding in HCN channels.
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Books on the topic "Cyclic nucleotide-gated channel"

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Goulding, Evan Hayward. Structure and function of the cyclic nucleotide-gated ion channels. 1994.

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Book chapters on the topic "Cyclic nucleotide-gated channel"

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Warren, René, and Robert S. Molday. "Regulation of the Rod Photoreceptor Cyclic Nucleotide-Gated Channel." In Advances in Experimental Medicine and Biology, 205–23. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0121-3_12.

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Grunwald, M. E., H. Zhong, and K. W. Yau. "Cyclic Nucleotide-Gated Channels: Classification, Structure and Function, Activators and Inhibitors." In Pharmacology of Ionic Channel Function: Activators and Inhibitors, 561–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-57083-4_22.

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Gupta, Vivek K., Ammaji Rajala, and Raju V. S. Rajala. "Ras-Associating Domain Proteins: A New Class of Cyclic Nucleotide-Gated Channel Modulators." In Retinal Degenerative Diseases, 777–82. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_99.

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Fitzgerald, J. Browning, Anna P. Malykhina, Muayyad R. Al-Ubaidi, and Xi-Qin Ding. "Functional Expression of Cone Cyclic Nucleotide-Gated Channel in Cone Photoreceptor-Derived 661W Cells." In Advances in Experimental Medicine and Biology, 327–34. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-74904-4_38.

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Ding, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori, and Hiroyuki Matsumoto. "Biochemical Characterization of Cone Cyclic Nucleotide-Gated (CNG) Channel Using the Infrared Fluorescence Detection System." In Retinal Degenerative Diseases, 769–75. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_98.

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Ding, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori, and Hiroyuki Matsumoto. "Exploration of Cone Cyclic Nucleotide-Gated Channel-Interacting Proteins Using Affinity Purification and Mass Spectrometry." In Retinal Degenerative Diseases, 57–65. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-3209-8_8.

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Ding, Xi-Qin, J. Browning Fitzgerald, Alexander B. Quiambao, Cynthia S. Harry, and Anna P. Malykhina. "Molecular Pathogenesis of Achromatopsia Associated with Mutations in the Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit." In Retinal Degenerative Diseases, 245–53. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_28.

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Conley, Shannon M., Xi-Qin Ding, and Muna I. Naash. "RDS in Cones Does Not Interact with the Beta Subunit of the Cyclic Nucleotide Gated Channel." In Retinal Degenerative Diseases, 63–70. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_8.

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Militante, Julius D., and John B. Lombardini. "Calcium Uptake in the Rat Retina is Dependent on the Function of the Cyclic Nucleotide-Gated Channel: Pharmacologic Evidence." In Advances in Experimental Medicine and Biology, 469–76. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46838-7_52.

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Nolan, Matthew F. "Hyperpolarization-Activated Cyclic Nucleotide Gated Channels." In Encyclopedia of Computational Neuroscience, 1413–17. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-6675-8_231.

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Conference papers on the topic "Cyclic nucleotide-gated channel"

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Chakraborty, Sonhita. "Cyclic Nucleotide-Gated Ion Channel 2 regulates auxin signaling and homeostasis." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1052927.

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Romanenko, A. S., L. A. Lomovatskaya, and N. V. Filinova. "SUBCELLULAR LOCALIZATION OF CYCLIC NUCLEOTIDE-GATED ION CHANNELS (CNGCS) IN THE POTATO ROOT CELLS IN THE BIOTIC STRESS." In The Second All-Russian Scientific Conference with international participation "Regulation Mechanisms of Eukariotic Cell Organelle Functions". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-318-1-106-108.

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Reports on the topic "Cyclic nucleotide-gated channel"

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Miller, Gad, and Jeffrey F. Harper. Pollen fertility and the role of ROS and Ca signaling in heat stress tolerance. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7598150.bard.

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The long-term goal of this research is to understand how pollen cope with stress, and identify genes that can be manipulated in crop plants to improve reproductive success during heat stress. The specific aims were to: 1) Compare heat stress dependent changes in gene expression between wild type pollen, and mutants in which pollen are heat sensitive (cngc16) or heat tolerant (apx2-1). 2) Compare cngc16 and apx2 mutants for differences in heat-stress triggered changes in ROS, cNMP, and Ca²⁺ transients. 3) Expand a mutant screen for pollen with increased or decreased thermo-tolerance. These aims were designed to provide novel and fundamental advances to our understanding of stress tolerance in pollen reproductive development, and enable research aimed at improving crop plants to be more productive under conditions of heat stress. Background: Each year crop yields are severely impacted by a variety of stress conditions, including heat, cold, drought, hypoxia, and salt. Reproductive development in flowering plants is highly sensitive to hot or cold temperatures, with even a single hot day or cold night sometimes being fatal to reproductive success. In many plants, pollen tube development and fertilization is often the weakest link. Current speculation about global climate change is that most agricultural regions will experience more extreme environmental fluctuations. With the human food supply largely dependent on seeds, it is critical that we consider ways to improve stress tolerance during fertilization. The heat stress response (HSR) has been intensively studied in vegetative tissues, but is poorly understood during reproductive development. A general paradigm is that HS is accompanied by increased production of reactive oxygen species (ROS) and induction of ROS-scavenging enzymes to protect cells from excess oxidative damage. The activation of the HSR has been linked to cytosolic Ca²⁺ signals, and transcriptional and translational responses, including the increased expression of heat shock proteins (HSPs) and antioxidative pathways. The focus of the proposed research was on two mutations, which have been discovered in a collaboration between the Harper and Miller labs, that either increase or decrease reproductive stress tolerance in a model plant, Arabidopsis thaliana (i.e., cngc16--cyclic nucleotide gated channel 16, apx2-1--ascorbate peroxidase 2,). Major conclusions, solutions, achievements. Using RNA-seq technology, the expression profiles of cngc16 and apx2 pollen grains were independently compared to wild type under favourable conditions and following HS. In comparison to a wild type HSR, there were 2,776 differences in the transcriptome response in cngc16 pollen, consistent with a model in which this heat-sensitive mutant fails to enact or maintain a normal wild-type HSR. In a comparison with apx2 pollen, there were 900 differences in the HSR. Some portion of these 900 differences might contribute to an improved HSR in apx2 pollen. Twenty-seven and 42 transcription factor changes, in cngc16 and apx2-1, respectively, were identified that could provide unique contributions to a pollen HSR. While we found that the functional HS-dependent reprogramming of the pollen transcriptome requires specific activity of CNGC16, we identified in apx2 specific activation of flavonol-biosynthesis pathway and auxin signalling that support a role in pollen thermotolerance. Results from this study have identified metabolic pathways and candidate genes of potential use in improving HS tolerance in pollen. Additionally, we developed new FACS-based methodology that can quantify the stress response for individual pollen in a high-throughput fashion. This technology is being adapted for biological screening of crop plant’s pollen to identify novel thermotolerance traits. Implications, both scientific and agricultural. This study has provided a reference data on the pollen HSR from a model plant, and supports a model that the HSR in pollen has many differences compared to vegetative cells. This provides an important foundation for understanding and improving the pollen HSR, and therefor contributes to the long-term goal of improving productivity in crop plants subjected to temperature stress conditions. A specific hypothesis that has emerged from this study is that pollen thermotolerance can be improved by increasing flavonol accumulation before or during a stress response. Efforts to test this hypothesis have been initiated, and if successful have the potential for application with major seed crops such as maize and rice.
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