Control information (126) related to the reception of data (128) within a subframe (116) is transmitted over multiple subframes (113, 116) over multiple carrier (107, 108) from communication system infrastructure (102). A controller (134) in a mobile wireless communication device (104) reconstructs the control information (126) received over multiple subframes (113, 116) based on at least some control information (130) in a first physical control channel (118) in a first subframe (113) transmitted over a first carrier (107) and at least some other control information (132) in a second physical control channel (120) in a second subframe (116) transmitted over a second carrier (108).

In this paper, we investigated the interaction of hanatoxin with the Shaker Kv channel. In contrast to the inhibitory actions of the toxin on Kv2.1 channels investigated in previous studies (Swartz and MacKinnon, 1997a,b; Li-Smerin and Swartz, 1998, 2000, 2001; Lee et al., 2003; Wang et al., 2004; Phillips et al., 2005; Alabi et al., 2007; Bosmans et al., 2008), our results show that hanatoxin facilitates opening of the Shaker Kv channel by interacting with the paddle motif (Figs. 1-3), stabilizing the voltage sensor in the activated state (Fig. 5), and influencing the final opening transition to stabilize the open state of the pore (Figs. 4 and 6). Although the effects of hanatoxin on the G-V relations (Figs. 1 and 2), the kinetics of channel closure (Figs. 1 and 4), and the ILT channel (Fig. 6) could in part be explained by effects on the final opening transition in Shaker, the pronounced effects of the toxin on gating currents (Fig. 5) suggest that early transitions in the voltage sensors are ...

Sigma-Aldrichs Cell Signaling & Neuroscience Voltage-Gated Ion Channels. The majority of ion channels fall into two broad categories: voltage-gated ion channels (VGIC) and ligand-gated ion channels (LGIC). Members of the VGIC superfamily are usually closed at the resting potential of the cell.

The model of Hodgkin and Huxley 1952 for the activation of voltage-dependent potassium channels postulates that voltage controls the conductance of membranes by changing the equilibrium between two states (resting and activated) of four identical and independent charged membrane particles. This hypothesis was supported by the finding that potassium channels are composed of four subunits (MacKinnon 1991), each containing an S4 segment that consists of a sequence of basic residues conserved within the primary structure of voltage-gated ion channels, and therefore hypothesized to confer voltage sensitivity (Noda et al. 1984; Greenblatt et al. 1985; Guy and Seetharamulu 1986). The idea that S4 is the Hodgkin and Huxley voltage sensing gating particle has been supported by recent evidence based on S4 accessibility to internal and external solutions (Yang and Horn 1995; Larsson et al. 1996; Yang et al. 1996; Yusaf et al. 1996; Starace et al. 1997; Baker et al. 1998), on total gating charge ...

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A scrambling sequence generation method is disclosed for reference signals, data, and downlink and uplink control channels. The scrambling sequence generation method determines an initial seed value used to calculate the scrambling sequence. The initial seed value is based on different parameters relating to the to be transmitted signals, and some of these parameters are explicitly defined for New Radio.

TY - JOUR. T1 - Hypoxia modulates nitric oxide-induced regulation of NMDA receptor currents and neuronal cell death. AU - Gbadegesin, Muyiwa. AU - Vicini, Stefano. AU - Hewett, Sandra. AU - Wink, David A.. AU - Espey, Michael. AU - Pluta, Ryszard M.. AU - Colton, Carol A.. PY - 1999. Y1 - 1999. N2 - Nitric oxide (NO) released from a new chemical class of donors enhances N-methyl-D-aspartate (NMDA) channel activity. Using whole cell and single- channel patch-clamp techniques, we have shown that (Z)-1-[N(3-ammoniopropyl)- N-(n-propyl)amino]-NO (PAPA-NO) and diethylamine NO, commonly termed NONOates, potentiate the glutamate-mediated response of recombinant rat NMDA receptors(NR1/NR2A) expressed in HEK-293 cells. The overall effect is an increase in both peak and steady-state whole cell currents induced by glutamate. Single-channel studies demonstrate a significant increase in open probability but no change in the mean single-channel open time or mean channel conductance. Reduction in oxygen levels ...

Experiments are often performed to study the behaviour of a single ion channel in response to a perturbation produced by a step change (jump) in a variable that influences its equilibrium position, for example a voltage jump or jump in agonist concentration. It is also common to apply a rectangular pulse (consisting of an on jump followed by an off jump); for example brief concentration pulses are used to mimic synaptic transmission.. Assuming a general Markov mechanism for channel dynamics, we obtain theoretical probability distributions of observable characteristics that describe the non-stationary behaviour of single ion channels which are subject to a jump, or to a pulse of finite duration. These characteristics are such things as open times, shut times, first latency, burst length and length of activation. We concentrate particularly on jumps to or from a zero level of agonist, which necessitates some modification to the usual arguments to cope with having some absorbing sets of states. ...

Changes of the electrical charges across the surface cell membrane are absolutely necessary to maintain cellular homeostasis in physiological as well as in pathological conditions. The opening of ion channels alter the charge distribution across the surface membrane as they allow the diffusion of ions such as K+, Ca++, Cl−, Na+. Traditionally, voltage-gated ion channels (VGIC) are known to play fundamental roles in controlling rapid bioelectrical signaling including action potential and/or contraction. However, several investigations have revealed that these classes of proteins can also contribute significantly to cell mitotic biochemical signaling, cell cycle progression, as well as cell volume regulation. All these functions are critically important for cancer cell proliferation. Interestingly, a variety of distinct VGICs are expressed in different cancer cell types, including metastasis but not in the tissues from which these tumors were generated. Given the increasing evidence suggesting ...

Mammalian cells are equipped with a large number of ion channels with diverse activation mechanisms and/or modalities. Ion channels are mainly located in the plasma membrane and thus serve crucial molecular mechanisms that transduce extracellular physical, biochemical or biological signals to intracellular events via mediating the movement of ions, particularly Ca2+ entry to elevate the intracellular Ca2+ level. Ion channels are also found in the membrane of intracellular organelles and regulate the ion homeostasis in such intracellular compartments as well as the cytosol. As such, ion channels play an important role in a wide range of physiological processes, which are not restricted to cell excitability. Accumulating evidence show that alterations in the expression and/or function of both the ion-forming or auxiliary subunits occur in neoplastic and malignant cells, markedly influencing cell apoptosis, proliferation, migration and invasion. In addition, ion channels significantly modulate the function

Concentration-dependent biphasic effects of drugs on ion channel activity have been reported in a variety of preparations, usually with stimulatory effects seen at low concentrations followed by increasingly dominant inhibition at higher levels. Such behaviour is often interpreted as evidence for the existence of separate modulatory drug binding sites. We demonstrate in this paper that it is possible for biphasic effects to be produced in an allosteric model of a ligand-activated ion channel, where diffusion-limited binding of the modulatory drug is restricted to either a stimulatory or an inhibitory site (but not both) because of steric overlap. The possibility of such an interaction mechanism should be kept in mind when interpreting experimental data if stoichiometric evidence from complementary techniques suggests that only one drug molecule is bound per receptor/ion channel complex.. ...

A system that stores a color management transform, typically using a grid table, where one or more of the input channels represents parameters used to control the reproduction of the conventional color image channels. The invention augments the existing grid-table based transform structure with additional channels to control the operation of the color models involved. These additional channels are not the conventional calorimetric or colorant image channels such as red, green, and blue, but are to control other aspects of the color transformation, such as exposure level or saturation. The augmentation also includes identification information that identifies the type of control (exposure, grey component replacement, etc.) the extra channels provide.

The gating of voltage-gated ion channels is controlled by the arginine-rich S4 helix of the voltage-sensor domain moving in response to an external potential. Recent studies have suggested that S4 moves in three to four steps to open the conducting pore, thus visiting several intermediate conformations during gating. However, the exact conformational changes are not known in detail. For instance, it has been suggested that there is a local rotation in the helix corresponding to short segments of a 3(10)-helix moving along S4 during opening and closing. Here, we have explored the energetics of the transition between the fully open state (based on the X-ray structure) and the first intermediate state towards channel closing (C-1), modeled from experimental constraints. We show that conformations within 3 angstrom of the X-ray structure are obtained in simulations starting from the C-1 model, and directly observe the previously suggested sliding 3(10)-helix region in S4. Through systematic free ...

Correlations between the voltage-gated ion channels shal (A-C), CbNav (D-F), and shaker (G-I) and soma size, actin, and tubulin expression. Points represe

Voltage-gated potassium (KV) channels open in response to membrane depolarization and are present in many cell types. In excitable cells, KV channels serve as the primary mechanism of repolarization of action potentials, whereas in nonexcitable cells, KV channels control the cell resting potential. Given the role of KV channels, it is not surprising that they regulate many fundamental physiological processes and are therefore considered important therapeutic targets for treatment of autoimmune, metabolic, neurological, and cardiovascular disorders, as well as cancer (Wulff et al., 2009). Despite these facts, there has been limited success in the clinical development of therapeutic agents that target KV channels. One reason for this is that many of the small molecules identified to date lack true molecular selectivity across members of the KV and other ion channel families, which could significantly compromise their therapeutic index. The lack of ion channel selectivity seems to be due to binding ...

sick unanticipated rewards will quickly keep a download voltage-gated ion channels as drug targets (methods and principles in medicinal psychotherapy teamwork. We get included with Bookshout and evaluate investigating their couple as a happy outcry to honor our signs. Their App brings full-throated for sight on funds and heavenly types.

Voltage-dependent ion channels have been found in the plasma membrane of the yeast Saccharomyces cerevisiae. Ion channel activities were recorded from spheroplasts or patches of plasma membrane with the patch-clamp technique. The most prominent activities came from a set of potassium channels with the properties of activation by positive but not negative voltages, high selectivity for potassium over sodium ion, unit conductance of 20 picosiemens, inhibition by tetraethylammonium or barium ions, and bursting kinetics. ...

Some characteristic features of band structures, like the band degeneracy at high symmetry points or the existence of energy gaps, usually reflect the symmetry of the crystal or, more precisely, the symmetry of the wave vector group at the relevant points of the Brillouin zone. In this paper, we will illustrate this property by considering two-dimensional (2D)-hexagonal lattices characterized by a possible two-fold degenerate band at the K points with a linear dispersion (Dirac points). By combining scanning tunneling spectroscopy and angle-resolved photoemission, we study the electronic properties of a similar system: the Ag/Cu(111) interface reconstruction characterized by a hexagonal superlattice, and we show that the gap opening at the K points of the Brillouin zone of the reconstructed cell is due to the symmetry breaking of the wave vector group.

Voltage-dependent ion channels are gated by voltage sensors that show a switchlike response to voltage differences across the membrane. Tao et al. used mutagenesis, electrophysiology, and x-ray crystallography to gain insight into the molecular basis of this response in voltage-dependent potassium channels. An occluded site was identified that catalyzes translation of positive charges across the membrane. The closed channel appears to be associated with a distribution of conformations, depending on the degree of hyperpolarization of the membrane, whereas the open channel appears to be associated with a specific conformation. Thus, the transition of the ion channel from open to closed occurs over a very small voltage difference.. X. Tao, A. Lee, W. Limapichat, D. A. Dougherty, R. MacKinnon, A gating charge transfer center in voltage sensors. Science 328, 67-73 (2010). [Abstract] [Full Text] ...

101年公務人員特種考試關務人員考試、101年公務人員特種考試 移民行政人員考試及101年國軍上校以上軍官轉任公務人員考試試題 代號：11130 等 別： 三等關務人員考試 類（科）別： 藥事 科 目： 藥理學與藥物化學 一、請說明下列各專有名詞之異同處。（20 分） (一) Antagonist & Inverse agonist (二) Pharmacodynamic & Pharmacokinetic (三) Ligand-gated channels & Voltage-gated channels (四) Ionotropic receptors & Metabotropic receptors (五) Tachyphylaxis & Supersensitivity ...

TY - JOUR. T1 - Voltage-Dependent Inactivation of MscS Occurs Independently of the Positively Charged Residues in the Transmembrane Domain. AU - Nomura, Takeshi. AU - Sokabe, Masahiro. AU - Yoshimura, Kenjiro. PY - 2016. Y1 - 2016. N2 - MscS (mechanosensitive channel of small conductance) is ubiquitously found among bacteria and plays a major role in avoiding cell lysis upon rapid osmotic downshock. The gating of MscS is modulated by voltage, but little is known about how MscS senses membrane potential. Three arginine residues (Arg-46, Arg-54, and Arg-74) in the transmembrane (TM) domain are possible to respond to voltage judging from the MscS structure. To examine whether these residues are involved in the voltage dependence of MscS, we neutralized the charge of each residue by substituting with asparagine (R46N, R54N, and R74N). Mechanical threshold for the opening of the expressed wild-type MscS and asparagine mutants did not change with voltage in the range from -40 to +100 mV. By contrast, ...

The cell membranes of all organisms contain ion channels that permit ions to pass into or out of the cell, and these channels play extremely important roles in fundamental physiological processes such as heartbeats and the rapid conduction of signals along neurons. An important property of these ion channels is their selective conductivity-they selectively permit the passage of particular ions. For example, potassium channels more readily permit the passage of potassium ions than the passage of sodium ions, despite the fact that potassium ions are larger.

Neural activity depends on the kinetic properties of ion channels expressed in neurons. Small changes in these properties can dramatically affect synaptic integration, membrane excitability and circuit function. Like all biochemical processes, the kinetics of ion channels have an exponential temperature dependence and the exponent (the Q10) differs several-fold between ion channel types within species [1-3]. In warm-blooded animals such as mammals, deviations in temperature of only a few degrees Celsius can thus disrupt neural activity and lead to loss of consciousness or death. However, cold blooded animals, including all invertebrates, manage to survive and function despite temperature fluctuations of tens of degrees Celsius [1]. How is this robustness achieved? One possibility is that the self-regulating, activity-dependent mechanisms that maintain neuronal properties in cold-blooded animals operate in a way that specifically gives rise to temperature robustness. In this work we develop a ...

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Voltage-gated ion channels are present in the excitable cell membranes of heart, skeletal muscle, brain and nerve cells. Blocking or modulating such channels can have a therapeutic effect, or may interfere with normal cell function. As a result, compounds that affect voltage-gated ion channels are important targets in drug discovery.

NMDARs retained in circulating RBCs remain functional and keep responding to stimulation with glutamate, HCA, or NMDA as well as to the inhibition by MK-801 (Figs. 3-6). Calcium transport through the receptor is electrogenic, putting NMDARs in line with other calcium-transporting ion channels (Fig. 4). The number of such ion channels in RBC is rather limited and their molecular identity often remains unknown (28). Among the TRP channels, only TRPC6 is described in RBC (17). Furthermore, there is biochemical and functional evidence for a CaV2.1 channel (1, 71). There are numerous electrophysiological reports of Ca2+-permeable channels that can be grouped in two categories: nonselective voltage activated cation channels (NSVAC; e.g., Refs. 4, 29) and receptor-mediated channels (e.g., Refs. 13, 25). Although the I-V curve for NSVAC in whole cell conductance mode (55) differs from that shown in Fig. 4D, NMDARs and NSVACs have one common property. Both channels share the hysteresis of whole cell ...

Cobalt 20 and Cobalt 10 are offered as a base console with 5000 control channels and 4,096 outputs (8 universes of DMX512A). A single control channel may control only intensity (dimmers) or it may control a DMX-controlled device (moving light, LED, media server, etc ...

Cobalt 20 and Cobalt 10 are offered as a base console with 5000 control channels and 4,096 outputs (8 universes of DMX512A). A single control channel may control only intensity (dimmers) or it may control a DMX-controlled device (moving light, LED, media server, etc ...

By default it shows only the back button, after your started moving around pages the forward button enables. Try Firefox Safe Mode to see if the problem goes away. Safe Mode is a troubleshooting mode, which disables most add-ons. (If youre not using it, switch to the Default theme.) * On Windows you can open Firefox 4.0+ in Safe Mode by holding the Shift key when you open the Firefox desktop or Start menu shortcut. * On Mac you can open Firefox 4.0+ in Safe Mode by holding the option key while starting Firefox. * On Linux you can open Firefox 4.0+ in Safe Mode by quitting Firefox and then going to your Terminal and running: firefox -safe-mode (you may need to specify the Firefox installation path e.g. /usr/lib/firefox) * Or open the Help menu and click on the Restart with Add-ons Disabled... menu item while Firefox is running. [[Image:FirefoxSafeMode,width=520]] Once you get the pop-up, just select Start in Safe Mode [[Image:Safe Mode Fx 15 - Win]] If the ...

Adenoviral i-eag domains restored slow deactivation in hiPSC-CMs.Representative tail currents recorded from hiPSC-CMs infected by: A, WT hERG1a.Ad; B, hERG1a(R5

CACNB1 (calcium voltage-gated channel auxiliary subunit beta 1), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.

Business Overview from 10-K filing for Icagen, Inc.:. We are a biopharmaceutical company focused on the discovery, development and commercialization of novel orally-administered small molecule drugs that modulate ion channel targets. Ions are charged particles, such as sodium, potassium, calcium and chloride. Ion channels are protein structures found in virtually every cell of the human body. Ion channels span the cell membrane and regulate the flow of ions into and out of cells. There are currently over 35 drugs marketed by third parties for multiple indications that modulate ion channels according to data from IMS Health. We believe this demonstrates that ion channels are attractive drug targets. Utilizing our proprietary know-how and integrated scientific and drug development capabilities, we have identified multiple drug candidates that modulate ion channels. ...

An apparatus for establishing a re-usable, recurring, mechanical connection to an organ within a patient is provided. A body fluid cartridge exchange platform device includes a hollow cartridge platform housing with a first end having an opening. The platform housing can additionally have a second end with a second opening. The first opening and the second opening facilitate insertion of an exchange cartridge insert that sealably engages the housing. The first opening and the second opening additionally facilitate removal of the exchange cartridge insert. The exchange cartridge insert can facilitate a flow path between a first leg and a second leg of the platform housing, and can facilitate a flow path between the platform housing and an external location for medical procedure or drug delivery purposes.

TY - JOUR. T1 - A conserved glutamate is important for slow inactivation in K+ channels. AU - Larsson, H. Peter. AU - Elinder, Fredrik. N1 - Funding Information: We thank Drs Peter Århem, Peter Löw, Staffan Johansson, and Bo Rydqvist for discussions and suggestions. We are grateful to Stefan Plantman and Kristina Hasslund for some of the recordings and to Carol Larsson and Russell Hill for editing the manuscript. This work was supported by grants from the Swedish Medical Research Council (F. E. and P. L.)Åke Wibergs stiftelse (F. E. and P. L.), Magn. Bergvalls Stiftelse (F. E. and P. L.), the Swedish Society of Medicine (P. L.), and Jeanssons Stiftelser (P. L.). F. E. and P. L. have junior research positions at the Swedish Medical Research Council. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 2000. Y1 - 2000. N2 - Voltage-gated ion channels undergo slow inactivation during prolonged depolarizations. We investigated the role of a conserved glutamate at the extracellular ...

A pressure swing sorption system comprises first and second sorbing chambers each including first and second openings defining a gas flow path between them, a sorbent bed disposed in the gas flow path and having a sorption inlet region near the first opening, and a heater positioned near the sorption inlet region of the sorbent bed. A valve arrangement interconnects an intake, an exhaust, and the first openings of the first and second sorbing chambers and also interconnects an outlet and the second openings of the first and second sorbing chambers. A connecting apparatus connects an energy source external to the first and second sorbing chambers to the heaters of the first and second sorbing chambers. A controller coupled to the valve arrangement and the connecting apparatus simultaneously directs gas from the first sorbing chamber to the outlet and directs a portion of the outlet gas through the second sorbing chamber to the exhaust. The controller also provides energy from the energy source to the

Structural model of hERG channels. (a) Key elements of hERG channel topology illustrated using the X-ray structure of KvAP. Two of the four subunits comprising the tetrameric channel are shown. (b) Model of the pore portion of hERG channel. The P-S6 fragment is shown for a dimer. Aromatic residues Phe656 and Tyr652 are critical for hERG block by most known small molecule ligands. Polar residues Thr623 and Ser624 modulate the binding potency for a number of reported hERG blockers ...

Sumoylation has recently been recognized as an important mechanism of cellular activity but until now its 60-or-so known targets were primarily nuclear proteins, mostly involved in gene transcription. The findings expand the influence of SUMO-related activity in biology, Goldstein said, a great and exciting surprise. There is still a good deal that we dont understand about this system, he said, but now we know where to look and why we must go there. SUMO may very well act on other ion channels that have yet to reveal their function because they were silent like K2P1 ...

January 8, 2018. Subtype-selective modulation of ion channels is often important, but extremely difficult to achieve for drug development. Using Nav1.7 as an example, we show that this challenge could be attributed to poor design in ion channel assays, which fail to detect most potent and selective compounds and are biased toward nonselective mechanisms. By exploiting different drug binding sites and modes of channel gating, we successfully direct a membrane potential assay toward non-pore-blocking mechanisms and identify Nav1.7-selective compounds. Our mechanistic approach to assay design addresses a significant hurdle in Nav1.7 drug discovery and is applicable to many other ion channels. ...

Voltage-activated K+ channels are integral membrane proteins that open or close a K(+)-selective pore in response to changes in transmembrane voltage. Although the S4 region of these channels has been implicated as the voltage sensor, little is known about how opening and closing of the pore is acco …

TY - JOUR. T1 - Compound-induced block of ion channel pore function. T2 - Inward-rectifier potassium channels as a model. AU - Furutani, Kazuharu. AU - Hibino, Hiroshi. AU - Inanobe, Atsushi. AU - Kurachi, Yoshihisa. PY - 2009/12/1. Y1 - 2009/12/1. N2 - Small chemical compounds modulate ion channel functions. This is the reflection of ligand interactions with ion channels at their various sites. Many biophysical and biochemical researches have been performed on this subject and have provided important basic concepts on the structure-functional relationships of ion channels. Especially, ion channel blockers have been excellent tools for biophysical studies of ion channels and some of them are actually used for treating various diseases. The mechanisms underlying the blocking action of various chemical compounds, however, remain largely unknown at the atomic level, partly because of the promiscuous nature of the reaction. As one of the attempts to overcome the problem, we have adopted a novel ...

Voltage-gated ion channels play fundamental roles in excitable cells, such as neurons, where they enable electric signaling. Normally, this signaling is well controlled, but brain damage, alterations in the ionic composition of the extracellular solution, or dysfunctional ion channels can increase the electrical excitability thereby causing epilepsy. Voltage-gated ion channels are obvious targets for antiepileptic drugs, and, as a rule of thumb, excitability is dampened either by closing voltagegated sodium channels (Nav channels) or by opening voltage-gated potassium channels (Kv channels). For example, several classical antiepileptic drugs block the ion-conducting pore of Nav channels. Despite the large number of existing antiepileptic drugs, one third of the patients with epilepsy suffer from intractable or pharmacoresistant seizures.. Our research group has earlier described how different polyunsaturated fatty acids (PUFAs) open a Kv channel by binding close to the voltage sensor and, from ...

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Voltage-gated ion channels generate electrical activity in excitable cells. As such, they are essential components of neuromuscular and neuronal systems, and are targeted by toxins from a wide variety of phyla, including the cnidarians. Here, we review cnidarian toxins known to target voltage-gated ion channels, the specific channel types targeted, and, where known, the sites of action of cnidarian toxins on different channels.

Looking for online definition of potassium voltage-gated channel, KQT-like subfamily, member 5 in the Medical Dictionary? potassium voltage-gated channel, KQT-like subfamily, member 5 explanation free. What is potassium voltage-gated channel, KQT-like subfamily, member 5? Meaning of potassium voltage-gated channel, KQT-like subfamily, member 5 medical term. What does potassium voltage-gated channel, KQT-like subfamily, member 5 mean?

Looking for online definition of potassium voltage-gated channel Shal-related subfamily member 1 in the Medical Dictionary? potassium voltage-gated channel Shal-related subfamily member 1 explanation free. What is potassium voltage-gated channel Shal-related subfamily member 1? Meaning of potassium voltage-gated channel Shal-related subfamily member 1 medical term. What does potassium voltage-gated channel Shal-related subfamily member 1 mean?

It is clear that the voltage--‐gated proton channel HVCN1 plays an essential role in a range of cell types, in particular immune cells. Previous published work has confirmed the existence of proton channels in both murine and human macrophages. However, the role of HVCN1 in macrophages has not been investigated. Given that the current literature on voltage--‐gated proton channels in immune cells has found HVCN1 to be involved in several cellular processes (such as the respiratory burst and signalling events) it is important to establish its functional role in macrophages, which are a crucial constituent of the immune system. The aim of my thesis was to investigate the function of voltage--‐gated proton channels in macrophages with the use of mice with a disrupting mutation within the Hvcn1 gene, which results in HVCN1 loss. In particular, I wanted to address how Hvcn1--‐/--‐ macrophages responded to LPS activation. I hypothesised that HVCN1 regulates the respiratory burst of ...

My dissertation work has focused on identifying regulatory mechanisms that govern Cyclic Guanosine Monophosphate (cGMP)-activation of Aquaprorin-1 (Aqp1) ion channels. Aquaporins serve as pores for water thus allowing enhanced water permeability in biological membranes (Preston, et al., 1992). A subset of Aquaporin proteins behave as ion channels regulated by intracellular signaling pathways (Anthony, et al., 2000; Ehring, et al., 1990; Yasui, et al., 1999a). cGMP is necessary for Aqp1 ion channel activation, but only a small subpopulation of Aqp1 proteins function as cGMP-activated ion channels . This observation indicates the involvement of additional regulatory mechanisms in the gating Aqp1 ion channels. Work from this dissertation provides the first insight into the potential mechanism that dictates Aqp1 ion channel availability to respond to the cGMP signal. I show here that insulin-activated tyrosine kinases positively regulate cGMP-mediated activation of Aqp1 ion channels when expressed ...

The voltage sensing domain (VSD) of the voltage-gated proton channel Hv1 mediates a H(+)-selective conductance that is coordinately controlled by the membrane potential (V) and the transmembrane pH gradient (ΔpH). Allosteric control of Hv1 channel opening by ΔpH (V-ΔpH coupling) is manifested by a characteristic shift of approximately 40 mV per ΔpH unit in the activation. To further understand the mechanism for V-ΔpH coupling in Hv1, H(+) current kinetics of activation and deactivation in excised membrane patches were analyzed as a function of the membrane potential and the pH in the intracellular side of the membrane (pHI). In this study, it is shown for the first time to our knowledge that the opening of Hv1 is preceded by a voltage-independent transition. A similar process has been proposed to constitute the step involving coupling between the voltage-sensing and pore domains in tetrameric voltage-gated channels. However, for Hv1, the VSD functions as both the voltage sensor and the conduction

BK channels regulate vascular tone by hyperpolarizing smooth muscle in response to fluctuating calcium concentrations. Oestrogen has been reported to lower blood pressure by increasing BK channel open probability through direct binding to the regulatory beta1-subunit(s) associated with the channel. The present investigation demonstrates that 17beta-oestradiol activates the BK channel complex by increasing the burst duration of channel openings. A subconductance state was observed in 25% of recordings following the addition of 17beta-oestradiol and could reflect uncoupling between the pore forming alpha1-subunit and the regulatory beta1-subunit. We also present evidence that more than one beta1-subunit is required to facilitate binding of 17beta-oestradiol to the channel complex.

2. A method as set forth in claim 1, wherein the occluder comprises a first collapsible and expandable screen and a second collapsible and expandable screen, wherein the two screens are connected with one another by means of a stud, wherein the expansion of the two screens occurs through self-actuation by means of a pre-tensing or a shape-memory device upon pushing the occluder out of the control channel, and wherein the application of the occluder includes the following steps:pushing the first screen out of the control channel by means of the control wire and in so doing expanding the first screen on the exit side of the incision while the second screen remains in the control channel (first application step),moving the gastroscope in such a way that the first screen comes into contiguity with the peripheral area of the incision on its exit side (second application step),moving the gastroscope in such a way that the second screen exits from the control channel and expands (third application step ...

Phosphatidic acid influences the gating of voltage-gated K+ channels through a non-specific surface charge mechanism and through a specific interaction between a voltage sensor arginine and the primary phosphate head group on the cytoplasmic membrane leaflet.

This Research Topic is cross-listed in the Frontiers in Physiology section: Membrane Physiology and Membrane Biophysics and the Frontiers in Pharmacology section: Pharmacology of Ion Channels and Channelopathies Ion channels are specialized membrane proteins responsible for the ions fluxes across the membrane of all cells of the human body. They open in response to voltage changes or binding of a chemical messenger, such as a neurotransmitter (i.e. ligand-gated ion channels). These proteins play heterogeneous and often critical physiological roles in both excitable and non-excitable cells, such as impulse generation and propagation, synaptic transmission and plasticity, hormonal secretion, hearth rhythm, blood pressure regulation, salt-water balance, cell proliferation and survival, to mention a few. As a consequence, it is no surprise that defects in ion channels function may cause diverse and severe diseases collectively known as channelopathies, which

Alamethicin forms voltage-gated ion channels that have moderate cation-selectivity. The enhancement of the cation-selectivity by introducing negatively charged residues at positions 7 and 18 has been studied using the tethered homodimers of alamethicin with Q7 and E18 (di-alm-Q7E18) and its analog with E7 and Q18 (di-alm-E7Q18). In the dimeric peptides, monomer peptides are linked at the N-termini by a disulfide bond. Both the peptides formed long lasting ion channels at cis-positive voltages when added to the cis-side membrane. Their long open duration enabled us to obtain current-voltage (I-V(m)) relations and reversal potentials at the single-channel level by applying a voltage ramp during the channel opening. The reversal potentials measured in asymmetric KCl solutions indicated that ionized E7 provided strong cation-selectivity, whereas ionized E18 little influenced the charge selectivity. This was also the case for the macroscopic charge selectivity determined from the reversal potentials obtained

In neuroscience, ball and chain inactivation is a model to explain the fast inactivation mechanism of voltage-gated ion channels. The process is also called hinged-lid inactivation or N-type inactivation. A voltage-gated ion channel can be in three states: open, closed, or inactivated. The inactivated state is mainly achieved through fast inactivation, by which a channel transitions rapidly from an open to an inactivated state. The model proposes that the inactivated state, which is stable and non-conducting, is caused by the physical blockage of the pore. The blockage is caused by a ball of amino acids connected to the main protein by a string of residues on the cytoplasmic side of the membrane. The ball enters the open channel and binds to the hydrophobic inner vestibule within the channel. This blockage causes inactivation of the channel by stopping the flow of ions. This phenomenon has mainly been studied in potassium channels and sodium channels. The initial evidence for a ball and chain ...

TY - JOUR. T1 - Molecular motions of the outer ring of charge of the sodium channel. T2 - Do they couple to slow inactivation?. AU - Xiong, Wei. AU - Li, Ronald A.. AU - Tian, Yanli. AU - Tomaselli, Gordon F.. PY - 2003/9/1. Y1 - 2003/9/1. N2 - In contrast to fast inactivation, the molecular basis of sodium (Na) channel slow inactivation is poorly understood. It has been suggested that structural rearrangements in the outer pore mediate slow inactivation of Na channels similar to C-type inactivation in potassium (K) channels. We probed the role of the outer ring of charge in inactivation gating by paired cysteine mutagenesis in the rat skeletal muscle Na channel (rNav1.4). The outer charged ring residues were substituted with cysteine, paired with cysteine mutants at other positions in the external pore, and coexpressed with rat brain β 1 in Xenopus oocytes. Dithiolthreitol (DTT) markedly increased the current in E403C+E758C double mutant, indicating the spontaneous formation of a disulfide ...

A transformed line of human embryonic kidney epithelial cells (HEK 293) is commonly used as an expression system for exogenous ion channel genes. Previously, it has been shown that these cells contain mRNAs for a variety of ion channels. Expression of some of these genes has been confirmed at the protein level. Patch-clamp electrophysiology experiments confirm the presence of multiple ion channels and molecular data agree with pharmacological profiles of identified channels. In this work, we show that endogenous voltage-gated potassium channels in HEK cells are a significant source of outward current at positive potentials. We show that both non-transfected HEK cells and HEK cells transfected with hyperpolarization-activated cyclic-nucleotide gated (HCN) channels have a significant amount of voltage-gated potassium (K(V)) current when certain tail current voltage-clamp protocols are used to assay HCN current activation. Specifically, tail current protocols that use a depolarized holding ...

The invention encompasses DRAM constructions, capacitor constructions, conductive contacts, integrated circuitry, methods of forming DRAM constructions, and methods of forming capacitor constructions. The invention includes a method of forming a contact to a node location comprising: a) forming an electrically insulative layer over a node location; b) patterning a masking layer over a portion of the insulative layer to form an unmasked portion and a masked portion of the insulative layer; c) removing parts of the masked and unmasked portions of the insulative layer to form a first opening over the node location which underlies a portion of the masking layer; d) forming an etch restriction layer within the first opening and over the masking layer; e) forming a sacrificial spacer layer within the first opening and over the etch restriction layer; f) forming a second opening extending from the first opening to the node location; and g) forming an electrically conductive pedestal within the first and second

Our work focuses on the molecular mechanisms underlying the robustness of neuronal activity. The properties of ion channels or synapses are dynamically regulated to maintain a stable level of activity, despite numerous external or internal disturbances. This stability depends on the dynamic regulation of various ion channels responsible for neuronal activity. We believe that dynamic processes regulate in a coordinated manner the properties of functionally-overlapping ion channels. We seek to determine the mechanisms responsible for the dynamic regulation of ion channels in the dopaminergic neurons of the substantia nigra pars compacta of rodents. These neurons are able to spontaneously generate regular activity patterns in the absence of any stimuli (including synaptic inputs). This pacemaker property allows us to precisely define their patterns of activity in vitro and to determine the causal relationships between the properties of the voltage-gated ion channels expressed by these neurons and ...

Only a few years ago, in 2011, the Sternson group exploited the properties of specialized domains to engineer new ligand-gated channels, which they called PSAMs2. First, the Sternson group made the critical observation that ligand-gated (i.e. molecule-sensing) ion channels can be divided into two somewhat independent domains, the ligand-binding domain and the ion channel domain. By screening candidate mutations in the ligand-binding domain of a starter channel, they were able to engineer the channel to lose its innate affinity to its natural ligand and acquire a preference for a synthetic molecule. By transplanting this new ligand binding domain onto other excitatory and inhibitory ion channel domains, the Sternson group successfully created novel excitatory and inhibitory channels. These channels now specialize in binding synthetic ligands that have never occurred in any biological system and are used as a tool to manipulate neuron activities.. Recent work by researchers in the Jan labs ...

T-type channels are distinguished from high voltage-activated (HVA)1 Ca2+ channels by their unique biophysical properties, including low voltage activation, fast activation and inactivation kinetics that produce a criss-crossing pattern between successive traces of a current-voltage (IV) protocol, slow deactivation kinetics, and tiny single channel conductance (Perez-Reyes [528], Armstrong [1237], Carbone [1238], Randall [340]).. Expression studies found that Cav3.3 channels generate currents with much slower activation and inactivation kinetics than Cav3.1 and Cav3.2 channels, which show the more typical transient kinetics described for native T-type channels (Perez-Reyes [528], Perez-Reyes [1239], Cribbs [1240], Lee [1241]).. Cav3.1 and Cav3.2 channels are activating and inactivating much faster than Cav3.3 channels. (Park [113]). The kinetics of T-type channels resemble those of Na+ channels, albeit on a slower time scale, suggesting that they may also inactivate by a ball-and-chain ...

Ion channels, which allow potassium and sodium ions to flow in and out of cells, are crucial in neuronal firing in the central nervous system and for brain and heart function. These channels use a ball-and-chain mechanism to help regulate their ion flow, according to a new study led by Weill Cornell Medicine scientists.. The study, published March 18, 2020, in Nature, confirms a long-standing hypothesis about ion channels, and represents a key advance in the understanding of the basic biological processes at work in most cells.. The direct imaging of the ball-and-chain mechanism, using electron-microscopy techniques, can also provide a new angle to design drugs that target it to improve ion channel function. Ion channel abnormalities have been linked to a long list of disorders including epilepsies, heart arrhythmias, schizophrenia and diabetes.. Scientists have been trying to get an atomic-scale picture of this mechanism since the 1970s, and now that we have it at last, it can become an ...

We built profiles based on hidden Markov models (HMMs) of each ion channel family (Fig. 1) (Yu and Catterall, 2004) using the sequences corresponding to the minimal pore structure (i.e., the pore loop and the flanking M1/S5 and M2/S6 transmembrane segments). We interrogated the nonredundant protein database, RefSeq of the National Center for Biotechnology Information, using each HMM profile (Yu et al., 2004). This search revealed 143 genes that encode related ion channel proteins. The amino acid sequence relationships of their minimal pore structures are illustrated in Fig. 1. We found 21 proteins related to four-domain NaV and CaV channels; two novel two-domain relatives of ion channel proteins (TPC); 90 proteins related to one-domain voltage-gated potassium channels, including 40 KV channels, eight calcium-activated potassium (KCa) channels, 10 CNG and HCN channels, and 32 TRP channels and relatives; and 30 proteins related to the Kir and K2P channels. We verified that these families are ...

Voltage-gated Na+ channels have positively charged transmembrane helices, the S4 segments, that move in response to changes of membrane voltage, driving conformational changes within each channel that open or close its activation gate. According to current views (1, 2), conformational changes in each of the four domains of a Na+ channel, or each subunit of a K+ channel, are followed by a concerted step, a single event, that opens the gate, allowing flux through the pore. The S4 movements associated with the early conformational changes have been detected with labeling experiments (3, 4), but the nature of the concerted step is unknown. In this paper and the following one, the possibility is explored that the concerted step for a Na+ channel consists of liberating a calcium ion bound in the channel lumen.. Calcium and other divalent cations have well-documented effects on the properties of Na+ channels (5). These effects were conveniently summarized by Frankenhaueser and Hodgkin (6), who said ...

MAIN CONCLUSION: Potassium-permeable slow activating vacuolar channels (SV) and chloride-permeable channels in the vacuole of the liverwort Marchantia polymorpha were characterized in respect to calcium dependence, selectivity, and pharmacology. The patch-clamp method was used in the study of ion channel activity in the vacuoles from the liverwort Marchantia polymorpha. The whole-vacuole recordings allowed simultaneous observation of two types of currents-predominant slow activated currents recorded at positive voltages and fast activated currents recorded at negative voltages. Single-channel recordings carried out in the gradient of KCl indicated that slow activated currents were carried by potassium-permeable slowly activating vacuolar channels (SV) and fast activated currents-by chloride-permeable channels. Both types of the channels were dependent in an opposite way on calcium, since elimination of this ion from the cytoplasmic side caused inhibition of SV channels, but the open probability ...

The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. He …

Typically the activities of the ion channels are not called firing patterns as in neuroscience we refer to firing when we mean the elicitation of action potentials (spikes) but yes: Whenever an AP was fired a sufficient amount of sodium channels had to be open and therefore I thing your reasoning is correct. In other terms what you are saying is that the effective channel conductances change during an action potential.. On your conclusion: In the regime of natural parameters the time scale of firing pattern 1 mostly depends on the time constants of the voltage gated ion channels and not so much on the absolute number of channels (especially if all the conductances would scale equally). In the world of Hodgin-Huxley like coupled- and nonlinear-dynamical systems the voltage does not scale strictly linear with increasing the participating max. conductances. The interplay of max. conductance and temporal gating dynamics resulting in the effective conductance itself depends on the voltage and there ...

Hi! I hope youll allow what might be a simple question to some of you, but I havent been able to find answers elsewhere. With a multisubunit ion channel, where the subunits have multiple transmembrane helices, how do you tell which of a subunits helices is the porelining helix? And what are the features that predict cation/anion selectivity? Does this have something to do with the amino acid sequence or is it more complex? I just finished an introductory lecture series on it, but the lecturer wasnt very clear. She used the acetylcholine receptor as an example, and said something about a 9 leucine, but I cant find an explanation of that term anyway. And how does that relate to ligand-gated channels in general ...

Ion channels are proteins that traverse the cell membrane and form gated pores that open and close in response to various stimuli. In order to experimentally probe aspects of ion channel functionality, we performed subtle structure function studies using the in vivo nonsense suppression method, which allows for the incorporation of synthetically accessible unnatural amino acids and hydroxy acids into an ion channel at a site of interest. Fluorinated aromatic amino acids are good probes for a cation-π interaction because fluorine substituents reduce the binding affinity of the aromatic for a cation in a linear, step-wise fashion. In collaboration with Professor Richard Horn at the Thomas Jefferson University, we substituted a series of fluorinated phenylalanines for important tyrosines in the Shaker B K+ channel and experimentally determined that TEA was binding to the residues through a cation-π interaction. We also determined that Ca2+ binds to and blocks the NaV1.4 channel through a ...

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Nanion offers analysis instruments for ion channel analysis, as patch clamp, impedance and bilayer recordings, used for drug development as cardiac safety and basic research.

The fourth transmembrane helix (S4) is the primary voltage-sensor of voltage-gated ion channels. Recent studies have used fluorescence resonance energy transfer as a spectroscopic ruler to determine the nature and magnitude of the voltage-induced movement of S4 that leads to channel opening.

It plots for me Hodgkin-Huxley activation and inactivation curves. A little explanation: The Hodgkin-Huxley formalism is a way to describe how neurons transmit signals. Neurons transmit signals by electric impulses. There is always a voltage difference between the interior and the exterior of the cell(called membrane potential). If i change this potential somewhere, this temporary change will spread across the cells surface, like a wave. The mechanisms responsible for this process are molecules in the cell membrane(called ion channels), which can open to let ions flow trough, which causes change in the membrane potential. There are tons of different ion channels, but most of them can be described with the Hodgkin-Huxley formalism. These curves describe how much will be these channels open ( 0-closed; 1-fully open) at different membrane potential values. To make things more complicated each ion channel is modeled by 2 curves (activation and inactivation) and the product at a current membrane ...

It plots for me Hodgkin-Huxley activation and inactivation curves. A little explanation: The Hodgkin-Huxley formalism is a way to describe how neurons transmit signals. Neurons transmit signals by electric impulses. There is always a voltage difference between the interior and the exterior of the cell(called membrane potential). If i change this potential somewhere, this temporary change will spread across the cells surface, like a wave. The mechanisms responsible for this process are molecules in the cell membrane(called ion channels), which can open to let ions flow trough, which causes change in the membrane potential. There are tons of different ion channels, but most of them can be described with the Hodgkin-Huxley formalism. These curves describe how much will be these channels open ( 0-closed; 1-fully open) at different membrane potential values. To make things more complicated each ion channel is modeled by 2 curves (activation and inactivation) and the product at a current membrane ...

Gene Information Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release heart rate insulin secretion neuronal excitability epithelial electrolyte transport smooth muscle contraction and cell volume. This gene encodes a member of the potassium channel voltage-gated subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. It is activated at the onset of myoblast differentiation. The gene is highly expressed in brain and in myoblasts. Overexpression of the gene may confer a growth advantage to cancer cells and favor tumor cell proliferation. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms. [provided by RefSeq Jul 2008]. ...

The voltage-gated proton channel, Hv1, Hv1 or HVCN1 (273 aas) (Ramsey et al., 2006). Thr29 is a phosphorylation site that activates the HVCN1 channel in leukocytes (Musset et al., 2010). The condctivity pore has been delineated and depends of a carboxyl group (Asp or Glu) in the channel (Morgan et al. 2013). The four transmembrane helices sense voltage and the pH gradient, and conduct protons exclusively. Selectivity is achieved by the unique ability of H3O+ to protonate an Asp-Arg salt bridge. Pathognomonic sensitivity of gating to the pH gradient ensures HV1 channel opening only when acid extrusion will result, which is crucial to its biological functions (DeCoursey 2015). An exception occurs in dinoflagellates (see 1.A.51.1.4) in which H+ influx through HV1 triggers a bioluminescent flash. The gating mechanism of Hv1, cooperativity within dimers and the sensitivity to metal ions have been reviewed (Okamura et al. 2015). How this channel is activated by cytoplasmic [H+] and depolarization of ...

A catheter is insertable into a vessel within a mammalian body. The catheter includes a tubular body, at least one channel extending along the tubular body; and a central lumen. The tubular body includes an exterior surface, a first end and a second end, and defines a length between the first end and the second end. The channel passes between a first opening and a second opening and includes a slot in the tubular body between the channel and the exterior surface of the tubular body such that a tubular member can be passed between the channel and the exterior surface. The slot extends from the first opening to the second opening and includes a pair of edges. The central lumen extends along the tubular body at least for a portion of the length of the tubular body. The catheter can be used as a rapid exchange catheter, for stent deployment, for drug delivery or therapeutic infusion with or without electroporation, to provide localized heat, to provide ultrasonic visualization and ablation, and to examine

0101] In another embodiment, a new cell-specific scrambling sequence, cnew, of 54NCCE in length, is defined for the advanced PDCCHs. The block of bits b.sup.(i)(0), . . . , b.sup.(i)(Mbit.sup.(i)-1) on each of the control channels to be transmitted in a subframe, where Mbit.sup.(i) is the number of bits in one subframe to be transmitted on physical downlink control channel number i, is multiplexed, resulting in a block of bits)) b.sup.(0)(0), . . . , b.sup.(0)(Mbit.sup.(0)-1), b.sup.(1)(0), . . . , b.sup.(1)(Mbit.sup.(1)-1), . . . , b.sup.(nPDCCH-1)(0), . . . , b.sup.(nPDCCH-1)(Mbit.sup.(nPDCCH-1)-1), where nPDCCH is the total number of PDCCHs transmitted in the subframe and nPDCCH=nPDCCHlegacy+nPDCCHnew, where nPDCCHlegacy and nPDCCHnew are the number of legacy PDCCHs and the number of new PDCCHs, respectively. The block of bits b.sup.(0)(0), . . . , b.sup.(0)(Mbit.sup.(0)-1), b.sup.(1)(0), . . . , b.sup.(1)(Mbit.sup.(1)-1), . . . , b.sup.(nPDCCH-1)(0), . . . , ...

Described here is a procedure for obtaining long stretches of current recording from one ion channel with the cell-attached patch-clamp ...

Electrical signaling in living cells controls a wide variety of arguably important physiological processes such as feeling, thinking, and heartbeat. Electrophysiological signals are created by proteins known as ion channels, and modulating the behavior of ion channels will alter the processes they control. The goal of my research program is to develop modulators selective for ion channel subtypes, to more precisely alter electrophysiological signals and identify channel subunits that generate native currents. Establishing the molecular identity of voltage-gated potassium (Kv) channels has been a particularly challenging problem: mammalian channels arise from a family of more than 40 genes, and pore-forming subunits can assemble as heterotetramers. Despite substantial and enduring efforts, few modulators of Kv channel activity have been discovered that are highly selective between channel subtypes. This is perhaps due to a high degree of sequence conservation between subfamily members in ...

Insulin exocytosis is regulated by ion channels that control excitability and Ca2+ influx. Channels also play an increasingly appreciated role in microdomain structure. In this study, we examine the mechanism by which the voltage-dependent K+ (Kv) channel Kv2.1 (KCNB1) facilitates depolarization-induced exocytosis in INS 832/13 cells and β-cells from human donors with and without type 2 diabetes (T2D). We find that Kv2.1, but not Kv2.2 (KCNB2), forms clusters of 6-12 tetrameric channels at the plasma membrane and facilitates insulin exocytosis. Knockdown of Kv2.1 expression reduces secretory granule targeting to the plasma membrane. Expression of the full-length channel (Kv2.1-wild-type) supports the glucose-dependent recruitment of secretory granules. However, a truncated channel (Kv2.1-ΔC318) that retains electrical function and syntaxin 1A binding, but lacks the ability to form clusters, does not enhance granule recruitment or exocytosis. Expression of KCNB1 appears reduced in T2D islets, ...

What is difference between Ion Channel and Transporter? Ion channel involves in passive transportation of ions while, transporter involves active transportation

Ligand-gated ion channels (LGICs) are a group of transmembrane ion channel proteins which open to allow ions such as Na+, K+, Ca2+, or Cl- t ...

Page contains details about calcein-loaded mechanosensitive channel of large conductance proteoliposomes . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com

The single-span membrane protein KCNE3 modulates a variety of voltage-gated ion channels in diverse biological contexts. In epithelial cells, KCNE3 regulates the function of the KCNQ1 potassium ion (K(+)) channel to enable K(+) recycling coupled to transepithelial chloride ion (Cl(-)) secretion, a physiologically critical cellular transport process in various organs and whose malfunction causes diseases, such as cystic fibrosis (CF), cholera, and pulmonary edema. Structural, computational, biochemical, and electrophysiological studies lead to an atomically explicit integrative structural model of the KCNE3-KCNQ1 complex that explains how KCNE3 induces the constitutive activation of KCNQ1 channel activity, a crucial component in K(+) recycling. Central to this mechanism are direct interactions of KCNE3 residues at both ends of its transmembrane domain with residues on the intra- and extracellular ends of the KCNQ1 voltage-sensing domain S4 helix. These interactions appear to stabilize the ...

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