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Journal articles on the topic 'KCNQ channels'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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1

Pattnaik, Bikash R., and Bret A. Hughes. "Effects of KCNQ channel modulators on the M-type potassium current in primate retinal pigment epithelium." American Journal of Physiology-Cell Physiology 302, no. 5 (2012): C821—C833. http://dx.doi.org/10.1152/ajpcell.00269.2011.

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Recently, we demonstrated the expression of KCNQ1, KCNQ4, and KCNQ5 transcripts in monkey retinal pigment epithelium (RPE) and showed that the M-type current in RPE cells is blocked by the specific KCNQ channel blocker XE991. Using patch-clamp electrophysiology, we investigated the pharmacological sensitivity of the M-type current in isolated monkey RPE cells to elucidate the subunit composition of the channel. Most RPE cells exhibited an M-type current with a voltage for half-maximal activation of approximately −35 mV. The M-type current activation followed a double-exponential time course an

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2

Gamper, Nikita, Yang Li, and Mark S. Shapiro. "Structural Requirements for Differential Sensitivity of KCNQ K+ Channels to Modulation by Ca2+/Calmodulin." Molecular Biology of the Cell 16, no. 8 (2005): 3538–51. http://dx.doi.org/10.1091/mbc.e04-09-0849.

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Calmodulin modulation of ion channels has emerged as a prominent theme in biology. The sensitivity of KCNQ1–5 K+ channels to modulation by Ca2+/calmodulin (CaM) was studied using patch-clamp, Ca2+ imaging, and biochemical and pharmacological approaches. Coexpression of CaM in Chinese hamster ovary (CHO) cells strongly reduced currents of KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3. In simultaneous current recording/Ca2+ imaging experiments, CaM conferred Ca2+ sensitivity to KCNQ4 and KCNQ5, but not to KCNQ1, KCNQ3, or KCNQ1/KCNE1 channels. A chimera constructed from the carboxy terminus of

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3

Brueggemann, Lioubov I., Jennifer M. Haick, Samantha Neuburg та ін. "KCNQ (Kv7) potassium channel activators as bronchodilators: combination with a β2-adrenergic agonist enhances relaxation of rat airways". American Journal of Physiology-Lung Cellular and Molecular Physiology 306, № 6 (2014): L476—L486. http://dx.doi.org/10.1152/ajplung.00253.2013.

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KCNQ (Kv7 family) potassium (K+) channels were recently found in airway smooth muscle cells (ASMCs) from rodent and human bronchioles. In the present study, we evaluated expression of KCNQ channels and their role in constriction/relaxation of rat airways. Real-time RT-PCR analysis revealed expression of KCNQ4 > KCNQ5 > KCNQ1 > KCNQ2 > KCNQ3, and patch-clamp electrophysiology detected KCNQ currents in rat ASMCs. In precision-cut lung slices, the KCNQ channel activator retigabine induced a concentration-dependent relaxation of small bronchioles preconstricted with methacholine (MeCh;

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4

Zhang, Xiaoming, Dongli Yang, and Bret A. Hughes. "KCNQ5/Kv7.5 potassium channel expression and subcellular localization in primate retinal pigment epithelium and neural retina." American Journal of Physiology-Cell Physiology 301, no. 5 (2011): C1017—C1026. http://dx.doi.org/10.1152/ajpcell.00185.2011.

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Previous studies identified in retinal pigment epithelial (RPE) cells an M-type K+ current, which in many other cell types is mediated by channels encoded by KCNQ genes. The aim of this study was to assess the expression of KCNQ genes in the monkey RPE and neural retina. Application of the specific KCNQ channel blocker XE991 eliminated the M-type current in freshly isolated monkey RPE cells, indicating that KCNQ subunits contribute to the underlying channels. RT-PCR analysis revealed the expression of KCNQ1, KCNQ4, and KCNQ5 transcripts in the RPE and all five KCNQ transcripts in the neural re

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5

Wang, Alice W., Michael C. Yau, Caroline K. Wang, et al. "Four drug-sensitive subunits are required for maximal effect of a voltage sensor–targeted KCNQ opener." Journal of General Physiology 150, no. 10 (2018): 1432–43. http://dx.doi.org/10.1085/jgp.201812014.

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KCNQ2-5 (Kv7.2–Kv7.5) channels are strongly influenced by an emerging class of small-molecule channel activators. Retigabine is the prototypical KCNQ activator that is thought to bind within the pore. It requires the presence of a Trp side chain that is conserved among retigabine-sensitive channels but absent in the retigabine-insensitive KCNQ1 subtype. Recent work has demonstrated that certain KCNQ openers are insensitive to mutations of this conserved Trp, and that their effects are instead abolished or attenuated by mutations in the voltage-sensing domain (VSD). In this study, we investigat

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6

Pablo, Juan Lorenzo, and Geoffrey S. Pitt. "FGF14 is a regulator of KCNQ2/3 channels." Proceedings of the National Academy of Sciences 114, no. 1 (2016): 154–59. http://dx.doi.org/10.1073/pnas.1610158114.

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KCNQ2/3 (Kv7.2/7.3) channels and voltage-gated sodium channels (VGSCs) are enriched in the axon initial segment (AIS) where they bind to ankyrin-G and coregulate membrane potential in central nervous system neurons. The molecular mechanisms supporting coordinated regulation of KCNQ and VGSCs and the cellular mechanisms governing KCNQ trafficking to the AIS are incompletely understood. Here, we show that fibroblast growth factor 14 (FGF14), previously described as a VGSC regulator, also affects KCNQ function and localization. FGF14 knockdown leads to a reduction of KCNQ2 in the AIS and a reduct

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7

Li, Yang, Paul Langlais, Nikita Gamper, Feng Liu, and Mark S. Shapiro. "Dual Phosphorylations Underlie Modulation of Unitary KCNQ K+Channels by Src Tyrosine Kinase." Journal of Biological Chemistry 279, no. 44 (2004): 45399–407. http://dx.doi.org/10.1074/jbc.m408410200.

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Src tyrosine kinase suppresses KCNQ (M-type) K+channels in a subunit-specific manner representing a mode of modulation distinct from that involving G protein-coupled receptors. We probed the molecular and biophysical mechanisms of this modulation using mutagenesis, biochemistry, and both whole-cell and single channel modes of patch clamp recording. Immunoprecipitation assays showed that Src associates with KCNQ2–5 subunits but phosphorylates only KCNQ3–5. Using KCNQ3 as a background, we found that mutation of a tyrosine in the amino terminus (Tyr-67) or one in the carboxyl terminus (Tyr-349) a

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8

Zhang, Fan, Yani Liu, Dandan Zhang, Xizhenzi Fan, Decheng Shao, and Han Li. "Suppression of KCNQ/M Potassium Channel in Dorsal Root Ganglia Neurons Contributes to the Development of Osteoarthritic Pain." Pharmacology 103, no. 5-6 (2019): 257–62. http://dx.doi.org/10.1159/000496422.

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Osteoarthritic pain has a strong impact on patients’ quality of life. Understanding the pathogenic mechanisms underlying osteoarthritic pain will likely lead to the development of more effective treatments. In the present study of osteoarthritic model rats, we observed a reduction of M-current density and a remarkable decrease in the levels of KCNQ2 and KCNQ3 proteins and mRNAs in dorsal root ganglia (DRG) neurons, which were associated with hyperalgesic behaviors. The activation of KCNQ/M channels with flupirtine significantly increased the mechanical threshold and prolonged the withdrawal la

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9

Schuetz, Friderike, Sharad Kumar, Philip Poronnik, and David J. Adams. "Regulation of the voltage-gated K+ channels KCNQ2/3 and KCNQ3/5 by serum- and glucocorticoid-regulated kinase-1." American Journal of Physiology-Cell Physiology 295, no. 1 (2008): C73—C80. http://dx.doi.org/10.1152/ajpcell.00146.2008.

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The voltage-gated KCNQ2/3 and KCNQ3/5 K+ channels regulate neuronal excitability. We recently showed that KCNQ2/3 and KCNQ3/5 channels are regulated by the ubiquitin ligase Nedd4-2. Serum- and glucocorticoid-regulated kinase-1 (SGK-1) plays an important role in regulation of epithelial ion transport. SGK-1 phosphorylation of Nedd4-2 decreases the ability of Nedd4-2 to ubiquitinate the epithelial Na+ channel, which increases the abundance of channel protein in the cell membrane. In this study, we investigated the mechanism(s) of SGK-1 regulation of M-type KCNQ channels expressed in Xenopus oocy

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10

Lagrange, Andre. "Retigabine: Bending Potassium Channels to Our Will." Epilepsy Currents 5, no. 5 (2005): 166–68. http://dx.doi.org/10.1111/j.1535-7511.2005.00052.x.

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The New Anticonvulsant Retigabine Favors Voltage-dependent Opening of the Kv7.2 (KCNQ2) Channel by Binding to Its Activation Gate Wuttke TV, Seebohm G, Bail S, Maljevic S, Lerche H Mol Pharmacol 2005;67:1009–1017 Retigabine (RTG) is an anticonvulsant drug with a novel mechanism of action. It activates neuronal KCNQ-type K+ channels by inducing a large hyperpolarizing shift of steady-state activation. To identify the structural determinants of KCNQ channel activation by RTG, we constructed a set of chimeras by using the neuronal KV7.2 ( KCNQ2) channel, which is activated by RTG, and the cardiac

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11

Lee, Sang-Yeon, Hyun Been Choi, Mina Park, et al. "Novel KCNQ4 variants in different functional domains confer genotype- and mechanism-based therapeutics in patients with nonsyndromic hearing loss." Experimental & Molecular Medicine 53, no. 7 (2021): 1192–204. http://dx.doi.org/10.1038/s12276-021-00653-4.

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AbstractLoss-of-function variant in the gene encoding the KCNQ4 potassium channel causes autosomal dominant nonsyndromic hearing loss (DFNA2), and no effective pharmacotherapeutics have been developed to reverse channel activity impairment. Phosphatidylinositol 4,5-bisphosphate (PIP2), an obligatory phospholipid for maintaining KCNQ channel activity, confers differential pharmacological sensitivity of channels to KCNQ openers. Through whole-exome sequencing of DFNA2 families, we identified three novel KCNQ4 variants related to diverse auditory phenotypes in the proximal C-terminus (p.Arg331Gln

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12

Hamilton, Kirk L., and Daniel C. Devor. "Basolateral membrane K+ channels in renal epithelial cells." American Journal of Physiology-Renal Physiology 302, no. 9 (2012): F1069—F1081. http://dx.doi.org/10.1152/ajprenal.00646.2011.

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The major function of epithelial tissues is to maintain proper ion, solute, and water homeostasis. The tubule of the renal nephron has an amazingly simple structure, lined by epithelial cells, yet the segments (i.e., proximal tubule vs. collecting duct) of the nephron have unique transport functions. The functional differences are because epithelial cells are polarized and thus possess different patterns (distributions) of membrane transport proteins in the apical and basolateral membranes of the cell. K+ channels play critical roles in normal physiology. Over 90 different genes for K+ channel

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13

Lombardo, Joseph, and Melissa A. Harrington. "Nonreciprocal mechanisms in up- and downregulation of spinal motoneuron excitability by modulators of KCNQ/Kv7 channels." Journal of Neurophysiology 116, no. 5 (2016): 2114–24. http://dx.doi.org/10.1152/jn.00446.2016.

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KCNQ/Kv7 channels form a slow noninactivating K+ current, also known as the M current. They activate in the subthreshold range of membrane potentials and regulate different aspects of excitability in neurons of the central nervous system. In spinal motoneurons (MNs), KCNQ/Kv7 channels have been identified in the somata, axonal initial segment, and nodes of Ranvier, where they generate a slow, noninactivating, K+ current sensitive to both muscarinic receptor-mediated inhibition and KCNQ/Kv7 channel blockers. In this study, we thoroughly reevaluated the function of up- and downregulation of KCNQ

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14

Yau, Michael C., Robin Y. Kim, Caroline K. Wang, et al. "One drug-sensitive subunit is sufficient for a near-maximal retigabine effect in KCNQ channels." Journal of General Physiology 150, no. 10 (2018): 1421–31. http://dx.doi.org/10.1085/jgp.201812013.

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Retigabine is an antiepileptic drug and the first voltage-gated potassium (Kv) channel opener to be approved for human therapeutic use. Retigabine is thought to interact with a conserved Trp side chain in the pore of KCNQ2–5 (Kv7.2–7.5) channels, causing a pronounced hyperpolarizing shift in the voltage dependence of activation. In this study, we investigate the functional stoichiometry of retigabine actions by manipulating the number of retigabine-sensitive subunits in concatenated KCNQ3 channel tetramers. We demonstrate that intermediate retigabine concentrations cause channels to exhibit bi

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15

Kim, Robin Y., Stephan A. Pless, and Harley T. Kurata. "PIP2 mediates functional coupling and pharmacology of neuronal KCNQ channels." Proceedings of the National Academy of Sciences 114, no. 45 (2017): E9702—E9711. http://dx.doi.org/10.1073/pnas.1705802114.

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Retigabine (RTG) is a first-in-class antiepileptic drug that suppresses neuronal excitability through the activation of voltage-gated KCNQ2–5 potassium channels. Retigabine binds to the pore-forming domain, causing a hyperpolarizing shift in the voltage dependence of channel activation. To elucidate how the retigabine binding site is coupled to changes in voltage sensing, we used voltage-clamp fluorometry to track conformational changes of the KCNQ3 voltage-sensing domains (VSDs) in response to voltage, retigabine, and PIP2. Steady-state ionic conductance and voltage sensor fluorescence closel

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16

Singh, Som P., Matthew William, Mira Malavia, and Xiang-Ping Chu. "Behavior of KCNQ Channels in Neural Plasticity and Motor Disorders." Membranes 12, no. 5 (2022): 499. http://dx.doi.org/10.3390/membranes12050499.

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The broad distribution of voltage-gated potassium channels (VGKCs) in the human body makes them a critical component for the study of physiological and pathological function. Within the KCNQ family of VGKCs, these aqueous conduits serve an array of critical roles in homeostasis, especially in neural tissue. Moreover, the greater emphasis on genomic identification in the past century has led to a growth in literature on the role of the ion channels in pathological disease as well. Despite this, there is a need to consolidate the updated findings regarding both the pharmacotherapeutic and pathol

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17

Wu, Wendy W., C. Savio Chan, D. James Surmeier, and John F. Disterhoft. "Coupling of L-Type Ca2+ Channels to KV7/KCNQ Channels Creates a Novel, Activity-Dependent, Homeostatic Intrinsic Plasticity." Journal of Neurophysiology 100, no. 4 (2008): 1897–908. http://dx.doi.org/10.1152/jn.90346.2008.

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Experience-dependent modification in the electrical properties of central neurons is a form of intrinsic plasticity that occurs during development and has been observed following behavioral learning. We report a novel form of intrinsic plasticity in hippocampal CA1 pyramidal neurons mediated by the KV7/KCNQ and CaV1/L-type Ca2+ channels. Enhancing Ca2+ influx with a conditioning spike train (30 Hz, 3 s) potentiated the KV7/KCNQ channel function and led to a long-lasting, activity-dependent increase in spike frequency adaptation—a gradual reduction in the firing frequency in response to sustain

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18

Gao, Haixia, Aurélien Boillat, Dongyang Huang, Ce Liang, Chris Peers, and Nikita Gamper. "Intracellular zinc activates KCNQ channels by reducing their dependence on phosphatidylinositol 4,5-bisphosphate." Proceedings of the National Academy of Sciences 114, no. 31 (2017): E6410—E6419. http://dx.doi.org/10.1073/pnas.1620598114.

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M-type (Kv7, KCNQ) potassium channels are proteins that control the excitability of neurons and muscle cells. Many physiological and pathological mechanisms of excitation operate via the suppression of M channel activity or expression. Conversely, pharmacological augmentation of M channel activity is a recognized strategy for the treatment of hyperexcitability disorders such as pain and epilepsy. However, physiological mechanisms resulting in M channel potentiation are rare. Here we report that intracellular free zinc directly and reversibly augments the activity of recombinant and native M ch

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19

Inanobe, Atsushi, Chizuru Tsuzuki, and Yoshihisa Kurachi. "An Epithelial Ca2+-Sensor Protein is an Alternative to Calmodulin to Compose Functional KCNQ1 Channels." Cellular Physiology and Biochemistry 36, no. 5 (2015): 1847–61. http://dx.doi.org/10.1159/000430155.

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Background/Aims: KCNQ channels transport K+ ions and participate in various cellular functions. The channels directly assemble with auxiliary proteins such as a ubiquitous Ca2+-sensor protein, calmodulin (CaM), to configure the physiological properties in a tissue-specific manner. Although many CaM-like Ca2+-sensor proteins have been identified in eukaryotes, how KCNQ channels selectively interact with CaM and how the homologues modulate the functionality of the channels remain unclear. Methods: We developed protocols to evaluate the interaction between the green fluorescent protein-tagged C-t

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20

Shorthouse, David, Lizhe Zhuang, Eric P. Rahrmann, et al. "KCNQ potassium channels modulate Wnt activity in gastro-oesophageal adenocarcinomas." Life Science Alliance 6, no. 12 (2023): e202302124. http://dx.doi.org/10.26508/lsa.202302124.

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Voltage-sensitive potassium channels play an important role in controlling membrane potential and ionic homeostasis in the gut and have been implicated in gastrointestinal (GI) cancers. Through large-scale analysis of 897 patients with gastro-oesophageal adenocarcinomas (GOAs) coupled with in vitro models, we findKCNQfamily genes are mutated in ∼30% of patients, and play therapeutically targetable roles in GOA cancer growth.KCNQ1andKCNQ3mediate the WNT pathway and MYC to increase proliferation through resultant effects on cadherin junctions. This also highlights novel roles ofKCNQ3in non-excit

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21

Wang, Caroline K., Shawn M. Lamothe, Alice W. Wang, Runying Y. Yang, and Harley T. Kurata. "Pore- and voltage sensor–targeted KCNQ openers have distinct state-dependent actions." Journal of General Physiology 150, no. 12 (2018): 1722–34. http://dx.doi.org/10.1085/jgp.201812070.

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Ion channels encoded by KCNQ2-5 generate a prominent K+ conductance in the central nervous system, referred to as the M current, which is controlled by membrane voltage and PIP2. The KCNQ2-5 voltage-gated potassium channels are targeted by a variety of activating compounds that cause negative shifts in the voltage dependence of activation. The underlying pharmacology of these effects is of growing interest because of possible clinical applications. Recent studies have revealed multiple binding sites and mechanisms of action of KCNQ activators. For example, retigabine targets the pore domain, b

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22

Gourgy-Hacohen, Orit, Polina Kornilov, Ilya Pittel, Asher Peretz, Bernard Attali, and Yoav Paas. "Capturing distinct KCNQ2 channel resting states by metal ion bridges in the voltage-sensor domain." Journal of General Physiology 144, no. 6 (2014): 513–27. http://dx.doi.org/10.1085/jgp.201411221.

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Although crystal structures of various voltage-gated K+ (Kv) and Na+ channels have provided substantial information on the activated conformation of the voltage-sensing domain (VSD), the topology of the VSD in its resting conformation remains highly debated. Numerous studies have investigated the VSD resting state in the Kv Shaker channel; however, few studies have explored this issue in other Kv channels. Here, we investigated the VSD resting state of KCNQ2, a K+ channel subunit belonging to the KCNQ (Kv7) subfamily of Kv channels. KCNQ2 can coassemble with the KCNQ3 subunit to mediate the IM

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23

Homma, Kazuaki. "The Pathological Mechanisms of Hearing Loss Caused by KCNQ1 and KCNQ4 Variants." Biomedicines 10, no. 9 (2022): 2254. http://dx.doi.org/10.3390/biomedicines10092254.

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Deafness-associated genes KCNQ1 (also associated with heart diseases) and KCNQ4 (only associated with hearing loss) encode the homotetrameric voltage-gated potassium ion channels Kv7.1 and Kv7.4, respectively. To date, over 700 KCNQ1 and over 70 KCNQ4 variants have been identified in patients. The vast majority of these variants are inherited dominantly, and their pathogenicity is often explained by dominant-negative inhibition or haploinsufficiency. Our recent study unexpectedly identified cell-death-inducing cytotoxicity in several Kv7.1 and Kv7.4 variants. Elucidation of this cytotoxicity m

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Wu, Zizhen, Gabor Toro, Guoying Xu, Danny Dang, Charmaine Prater, and Qing Yang. "Paclitaxel Inhibits KCNQ Channels in Primary Sensory Neurons to Initiate the Development of Painful Peripheral Neuropathy." Cells 11, no. 24 (2022): 4067. http://dx.doi.org/10.3390/cells11244067.

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Cancer patients undergoing paclitaxel infusion usually experience peripheral nerve degeneration and serious neuropathic pain termed paclitaxel-induced peripheral neuropathy (PIPN). However, alterations in the dose or treatment schedule for paclitaxel do not eliminate PIPN, and no therapies are available for PIPN, despite numerous studies to uncover the mechanisms underlying the development/maintenance of this condition. Therefore, we aimed to uncover a novel mechanism underlying the pathogenesis of PIPN. Clinical studies suggest that acute over excitation of primary sensory neurons is linked t

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Suh, Byung-Chang, Lisa F. Horowitz, Wiebke Hirdes, Ken Mackie, and Bertil Hille. "Regulation of KCNQ2/KCNQ3 Current by G Protein Cycling." Journal of General Physiology 123, no. 6 (2004): 663–83. http://dx.doi.org/10.1085/jgp.200409029.

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Receptor-mediated modulation of KCNQ channels regulates neuronal excitability. This study concerns the kinetics and mechanism of M1 muscarinic receptor–mediated regulation of the cloned neuronal M channel, KCNQ2/KCNQ3 (Kv7.2/Kv7.3). Receptors, channels, various mutated G-protein subunits, and an optical probe for phosphatidylinositol 4,5-bisphosphate (PIP2) were coexpressed by transfection in tsA-201 cells, and the cells were studied by whole-cell patch clamp and by confocal microscopy. Constitutively active forms of Gαq and Gα11, but not Gα13, caused a loss of the plasma membrane PIP2 and a t

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Gao, Lei, Hong Fei, Nathan C. Connors, Jiaming Zhang та Irwin B. Levitan. "Drosophila Ortholog of Succinyl-CoA Synthetase β Subunit: A Novel Modulator of Drosophila KCNQ Channels". Journal of Neurophysiology 99, № 5 (2008): 2736–40. http://dx.doi.org/10.1152/jn.01314.2007.

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Voltage-gated KCNQ potassium channels are responsible for slowly activating potassium currents in heart, brain, and other tissues. Functional defects of KCNQ channels are linked with many diseases, including epilepsy and cardiac arrhythmias. Therefore KCNQ potassium channels have been widely studied, especially in the CNS. We have identified Drosophila CG11963, which encodes a protein orthologous to the β subunit of mammalian succinyl-CoA synthetase (SCS, also known as succinate thiokinase), as a novel modulator of Drosophila KCNQ channels. Direct interaction of CG11963 and dKCNQ was demonstra

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Brueggemann, Lioubov I., Christopher J. Moran, John A. Barakat, Jay Z. Yeh, Leanne L. Cribbs, and Kenneth L. Byron. "Vasopressin stimulates action potential firing by protein kinase C-dependent inhibition of KCNQ5 in A7r5 rat aortic smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (2007): H1352—H1363. http://dx.doi.org/10.1152/ajpheart.00065.2006.

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[Arg8]-vasopressin (AVP), at low concentrations (10–500 pM), stimulates oscillations in intracellular Ca2+ concentration (Ca2+ spikes) in A7r5 rat aortic smooth muscle cells. Our previous studies provided biochemical evidence that protein kinase C (PKC) activation and phosphorylation of voltage-sensitive K+ (Kv) channels are crucial steps in this process. In the present study, Kv currents ( IKv) and membrane potential were measured using patch clamp techniques. Treatment of A7r5 cells with 100 pM AVP resulted in significant inhibition of IKv. This effect was associated with gradual membrane de

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28

Brown, David A., and Gayle M. Passmore. "Neural KCNQ (Kv7) channels." British Journal of Pharmacology 156, no. 8 (2009): 1185–95. http://dx.doi.org/10.1111/j.1476-5381.2009.00111.x.

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Tzingounis, Anastasios V. "SMITten for KCNQ Channels." Biophysical Journal 113, no. 3 (2017): 503–5. http://dx.doi.org/10.1016/j.bpj.2017.06.056.

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30

Gibor, Gilad, Daniel Yakubovich, Asher Peretz, and Bernard Attali. "External Barium Affects the Gating of KCNQ1 Potassium Channels and Produces a Pore Block via Two Discrete Sites." Journal of General Physiology 124, no. 1 (2004): 83–102. http://dx.doi.org/10.1085/jgp.200409068.

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The pore properties and the reciprocal interactions between permeant ions and the gating of KCNQ channels are poorly understood. Here we used external barium to investigate the permeation characteristics of homomeric KCNQ1 channels. We assessed the Ba2+ binding kinetics and the concentration and voltage dependence of Ba2+ steady-state block. Our results indicate that extracellular Ba2+ exerts a series of complex effects, including a voltage-dependent pore blockade as well as unique gating alterations. External barium interacts with the permeation pathway of KCNQ1 at two discrete and nonsequent

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Cavaliere, Sonia, and James J. L. Hodge. "Drosophila KCNQ Channel Displays Evolutionarily Conserved Electrophysiology and Pharmacology with Mammalian KCNQ Channels." PLoS ONE 6, no. 9 (2011): e23898. http://dx.doi.org/10.1371/journal.pone.0023898.

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Lambrecht, Nils W. G., Iskandar Yakubov, David Scott, and George Sachs. "Identification of the K efflux channel coupled to the gastric H-K-ATPase during acid secretion." Physiological Genomics 21, no. 1 (2005): 81–91. http://dx.doi.org/10.1152/physiolgenomics.00212.2004.

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Genomic microarray analysis of genes specifically expressed in a pure cell isolate from a heterocellular organ identified the likely K efflux channel associated with the gastric H-K-ATPase. The function of this channel is to supply K to the luminal surface of the pump to allow H for K exchange. KCNQ1-KCNE2 was the most highly expressed and significantly enriched member of the large variety of K channels expressed in the gastric epithelium. The function of this K channel in acid secretion was then shown by inhibition of secretion in isolated gastric glands with specific KCNQ inhibitors and by c

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Ohya, Susumu, Keiichi Asakura, Katsuhiko Muraki, Minoru Watanabe, and Yuji Imaizumi. "Molecular and functional characterization of ERG, KCNQ, and KCNE subtypes in rat stomach smooth muscle." American Journal of Physiology-Gastrointestinal and Liver Physiology 282, no. 2 (2002): G277—G287. http://dx.doi.org/10.1152/ajpgi.00200.2001.

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Contribution of K+ channels derived from the expression of ERG, KCNQ, and KCNE subtypes, which are responsible for rapidly and slowly activating delayed rectifier K+ currents ( I Kr and I Ks, respectively) in cardiac myocytes, to membrane currents was examined in stomach circular smooth muscle cells (SMCs). The region-qualified multicell RT-PCR showed that ERG1/KCNE2 transcripts were expressed in rat stomach fundus and antrum SMCs and that KCNQ1/KCNE1 transcripts were expressed in antrum but not fundus. Western blotting and immunocytochemical analyses indicate that ERG1 proteins were substanti

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Lee, Choongheon, J. Chris Holt, and Timothy A. Jones. "Effect of M-current modulation on mammalian vestibular responses to transient head motion." Journal of Neurophysiology 118, no. 6 (2017): 2991–3006. http://dx.doi.org/10.1152/jn.00384.2017.

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The precise role and mechanisms underlying efferent modulation of peripheral vestibular afferent function are not well understood in mammals. Clarifying the details of efferent action may lead to new strategies for clinical management of debilitating disturbances in vestibular and balance function. Recent evidence in turtle indicates that efferent modulation of M-currents is likely one mechanism for modifying afferent discharge. M-currents depend in part on KCNQ potassium conductances (Kv7), which can be adjusted through efferent activation of M1, M3, and/or M5 muscarinic acetylcholine recepto

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Suh, Byung-Chang, and Bertil Hille. "Does diacylglycerol regulate KCNQ channels?" Pflügers Archiv - European Journal of Physiology 453, no. 3 (2006): 293–301. http://dx.doi.org/10.1007/s00424-006-0092-3.

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Luo, Lei, Bowen Li, Sheng Wang, et al. "Centipedes subdue giant prey by blocking KCNQ channels." Proceedings of the National Academy of Sciences 115, no. 7 (2018): 1646–51. http://dx.doi.org/10.1073/pnas.1714760115.

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Centipedes can subdue giant prey by using venom, which is metabolically expensive to synthesize and thus used frugally through efficiently disrupting essential physiological systems. Here, we show that a centipede (Scolopendra subspinipes mutilans, ∼3 g) can subdue a mouse (∼45 g) within 30 seconds. We found that this observation is largely due to a peptide toxin in the venom, SsTx, and further established that SsTx blocks KCNQ potassium channels to exert the lethal toxicity. We also demonstrated that a KCNQ opener, retigabine, neutralizes the toxicity of a centipede’s venom. The study indicat

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Hawkins, Virginia E., Joanna M. Hawryluk, Ana C. Takakura, Anastasios V. Tzingounis, Thiago S. Moreira, and Daniel K. Mulkey. "HCN channels contribute to serotonergic modulation of ventral surface chemosensitive neurons and respiratory activity." Journal of Neurophysiology 113, no. 4 (2015): 1195–205. http://dx.doi.org/10.1152/jn.00487.2014.

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Chemosensitive neurons in the retrotrapezoid nucleus (RTN) provide a CO2/H+-dependent drive to breathe and function as an integration center for the respiratory network, including serotonergic raphe neurons. We recently showed that serotonergic modulation of RTN chemoreceptors involved inhibition of KCNQ channels and activation of an unknown inward current. Hyperpolarization-activated cyclic-nucleotide-gated (HCN) channels are the molecular correlate of the hyperpolarization-activated inward current ( Ih) and have a high propensity for modulation by serotonin. To investigate whether HCN channe

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Jow, Flora, Ru Shen, Pranab Chanda, et al. "Validation of a Medium-Throughput Electrophysiological Assay for KCNQ2/3 Channel Enhancers Using IonWorks HT." Journal of Biomolecular Screening 12, no. 8 (2007): 1059–67. http://dx.doi.org/10.1177/1087057107307448.

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Enhancers of KCNQ channels are known to be effective in chronic pain models. To discover novel enhancers of KCNQ channels, the authors developed a medium-throughput electrophysiological assay by using the IonWorks platform. Screening of 20 CHO-K1 clones stably expressing KCNQ2/3 was performed on the IonWorks HT until the best clone (judged from seal rate, current level, and stability) was obtained. The KCNQ2/3 current amplitude in the cells was found to increase from 60 ± 15 pA to 473 ± 80 pA (at —10 mV), and the expression rate was increased by 56% when the cells were incubated at 27 °C overn

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Suh, Byung-Chang, and Bertil Hille. "Electrostatic Interaction of Internal Mg2+ with Membrane PIP2 Seen with KCNQ K+ Channels." Journal of General Physiology 130, no. 3 (2007): 241–56. http://dx.doi.org/10.1085/jgp.200709821.

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Activity of KCNQ (Kv7) channels requires binding of phosphatidylinositol 4,5-bisphosphate (PIP2) from the plasma membrane. We give evidence that Mg2+ and polyamines weaken the KCNQ channel–phospholipid interaction. Lowering internal Mg2+ augmented inward and outward KCNQ currents symmetrically, and raising Mg2+ reduced currents symmetrically. Polyvalent organic cations added to the pipette solution had similar effects. Their potency sequence followed the number of positive charges: putrescine (+2) &lt; spermidine (+3) &lt; spermine (+4) &lt; neomycin (+6) &lt; polylysine (≫+6).

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Jepps, Thomas A., Iain A. Greenwood, James D. Moffatt, Kenton M. Sanders, and Susumu Ohya. "Molecular and functional characterization of Kv7 K+ channel in murine gastrointestinal smooth muscles." American Journal of Physiology-Gastrointestinal and Liver Physiology 297, no. 1 (2009): G107—G115. http://dx.doi.org/10.1152/ajpgi.00057.2009.

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Members of the Kv7 voltage-gated K+ channel family are important determinants of cardiac and neuronal membrane excitability. Recently, we and others have shown that Kv7 channels are also crucial regulators of smooth muscle activity. The aim of the present study was to assess the Kv7 expression in different parts of the murine gastrointestinal (GI) tract and to assess their functional roles by use of pharmacological agents. Of KCNQ/Kv7 members, both KCNQ4/Kv7.4 and KCNQ5/Kv7.5 genes and proteins were the most abundantly expressed Kv7 channels in smooth muscles throughout the GI tract. Immunohis

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Wei, Aguan D., Alice Butler, and Lawrence Salkoff. "KCNQ-like Potassium Channels inCaenorhabditis elegans." Journal of Biological Chemistry 280, no. 22 (2005): 21337–45. http://dx.doi.org/10.1074/jbc.m502734200.

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Mruk, Karen, Robert O. Blaustein, and William R. Kobertz. "Pinpointing Calmodulin on Functioning KCNQ Channels." Biophysical Journal 100, no. 3 (2011): 100a. http://dx.doi.org/10.1016/j.bpj.2010.12.751.

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Cooper, Edward C. "Potassium channels (including KCNQ) and epilepsy." Epilepsia 51 (December 2010): 10. http://dx.doi.org/10.1111/j.1528-1167.2010.02796.x.

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Evseev, Alexey I., Iurii Semenov, Robert Brenner, and Mark S. Shapiro. "Kcnq Channels in Airway Smooth Muscle." Biophysical Journal 104, no. 2 (2013): 269a. http://dx.doi.org/10.1016/j.bpj.2012.11.1511.

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Du, Canwei, Jiameng Li, Zicheng Shao, et al. "Centipede KCNQ Inhibitor SsTx Also Targets KV1.3." Toxins 11, no. 2 (2019): 76. http://dx.doi.org/10.3390/toxins11020076.

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It was recently discovered that Ssm Spooky Toxin (SsTx) with 53 residues serves as a key killer factor in red-headed centipede’s venom arsenal, due to its potent blockage of the widely expressed KCNQ channels to simultaneously and efficiently disrupt cardiovascular, respiratory, muscular, and nervous systems, suggesting that SsTx is a basic compound for centipedes’ defense and predation. Here, we show that SsTx also inhibits KV1.3 channel, which would amplify the broad-spectrum disruptive effect of blocking KV7 channels. Interestingly, residue R12 in SsTx extends into the selectivity filter to

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Cao, Yumei, David Bartolomé-Martín, Naama Rotem, et al. "Rescue of homeostatic regulation of striatal excitability and locomotor activity in a mouse model of Huntington’s disease." Proceedings of the National Academy of Sciences 112, no. 7 (2015): 2239–44. http://dx.doi.org/10.1073/pnas.1405748112.

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We describe a fast activity-dependent homeostatic regulation of intrinsic excitability of identified neurons in mouse dorsal striatum, the striatal output neurons. It can be induced by brief bursts of activity, is expressed on a time scale of seconds, limits repetitive firing, and can convert regular firing patterns to irregular ones. We show it is due to progressive recruitment of the KCNQ2/3 channels that generate the M current. This homeostatic mechanism is significantly reduced in striatal output neurons of the R6/2 transgenic mouse model of Huntington’s disease, at an age when the neurons

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Larsson, Peter. "Regulation of Voltage Sensor Movement in KCNQ Channels by KCNE Beta Subunits." Biophysical Journal 104, no. 2 (2013): 7a. http://dx.doi.org/10.1016/j.bpj.2012.11.065.

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Nakajo, Koichi, and Yoshihiro Kubo. "Mechanisms underlying subunit recognition and channel assembly in KCNQ channels." Neuroscience Research 58 (January 2007): S188. http://dx.doi.org/10.1016/j.neures.2007.06.832.

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Borgini, Matteo, Pravat Mondal, Ruiting Liu, and Peter Wipf. "Chemical modulation of Kv7 potassium channels." RSC Medicinal Chemistry 12, no. 4 (2021): 483–537. http://dx.doi.org/10.1039/d0md00328j.

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This review describes the synthetic and medicinal chemistry of small molecule modulators of the voltage-gated Kv7 (KCNQ) potassium channels and the available data of their biological and clinical properties.

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Li, Xiaofan, Hansi Liu, Jose Chu Luo, et al. "Major diversification of voltage-gated K+ channels occurred in ancestral parahoxozoans." Proceedings of the National Academy of Sciences 112, no. 9 (2015): E1010—E1019. http://dx.doi.org/10.1073/pnas.1422941112.

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We examined the origins and functional evolution of the Shaker and KCNQ families of voltage-gated K+ channels to better understand how neuronal excitability evolved. In bilaterians, the Shaker family consists of four functionally distinct gene families (Shaker, Shab, Shal, and Shaw) that share a subunit structure consisting of a voltage-gated K+ channel motif coupled to a cytoplasmic domain that mediates subfamily-exclusive assembly (T1). We traced the origin of this unique Shaker subunit structure to a common ancestor of ctenophores and parahoxozoans (cnidarians, bilaterians, and placozoans).

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