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Journal articles on the topic 'Voltage sensing domain'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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1

Sakata, Souhei, Makoto Matsuda, Akira Kawanabe, and Yasushi Okamura. "Domain-to-domain coupling in voltage-sensing phosphatase." Biophysics and Physicobiology 14 (2017): 85–97. http://dx.doi.org/10.2142/biophysico.14.0_85.

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2

Villalba-Galea, Carlos A. "Ph Sensitivity of Voltage Sensing Domain Relaxation." Biophysical Journal 106, no. 2 (January 2014): 745a—746a. http://dx.doi.org/10.1016/j.bpj.2013.11.4106.

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3

Rayaprolu, Vamseedhar, Perrine Royal, Karen Stengel, Guillaume Sandoz, and Susy C. Kohout. "Dimerization of the voltage-sensing phosphatase controls its voltage-sensing and catalytic activity." Journal of General Physiology 150, no. 5 (April 25, 2018): 683–96. http://dx.doi.org/10.1085/jgp.201812064.

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Multimerization is a key characteristic of most voltage-sensing proteins. The main exception was thought to be the Ciona intestinalis voltage-sensing phosphatase (Ci-VSP). In this study, we show that multimerization is also critical for Ci-VSP function. Using coimmunoprecipitation and single-molecule pull-down, we find that Ci-VSP stoichiometry is flexible. It exists as both monomers and dimers, with dimers favored at higher concentrations. We show strong dimerization via the voltage-sensing domain (VSD) and weak dimerization via the phosphatase domain. Using voltage-clamp fluorometry, we also find that VSDs cooperate to lower the voltage dependence of activation, thus favoring the activation of Ci-VSP. Finally, using activity assays, we find that dimerization alters Ci-VSP substrate specificity such that only dimeric Ci-VSP is able to dephosphorylate the 3-phosphate from PI(3,4,5)P3 or PI(3,4)P2. Our results indicate that dimerization plays a significant role in Ci-VSP function.

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4

Okamura, Yasushi, and Jack E. Dixon. "Voltage-Sensing Phosphatase: Its Molecular Relationship With PTEN." Physiology 26, no. 1 (February 2011): 6–13. http://dx.doi.org/10.1152/physiol.00035.2010.

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Voltage-sensing phosphoinositide phosphatase (VSP) contains voltage sensor and cytoplasmic phosphatase domains. A unique feature of this protein is that depolarization-induced motions of the voltage sensor activate PtdIns(3,4,5)P3and PtdIns(4,5)P2phosphatase activities. VSP exhibits remarkable structural similarities with PTEN, the phosphatase and tensin homolog deleted on chromosome 10. These similarities include the cytoplasmic phosphatase region, the phosphoinositide binding region, and the putative membrane interacting C2 domain.

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5

Gagnon, Dominique G., and Francisco Bezanilla. "The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers." Journal of General Physiology 136, no. 5 (October 25, 2010): 555–68. http://dx.doi.org/10.1085/jgp.201010487.

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Voltage-gated ion channels couple conformational change(s) of the voltage-sensing domain to those of the opening of an intracellular gate to allow ionic conduction. Much larger positive potentials are required to couple these conformational changes to the opening of the gate of Shaker K+ channels with the concurrent mutations V369I, I372L, and S376T (ILT) at the N-terminal end of the S4 segment. We used cut-open oocyte voltage clamp to study the biophysical and thermodynamical properties of heterotetrameric concatemerized channels with different stoichiometries of ILT mutations. The voltage-sensing domains of ILT mutant channels require smaller depolarization to activate but their intracellular gate does not immediately follow the movement of the voltage-sensing domain, requiring larger depolarization to open. Our results demonstrate that each subunit contributes equally to the rightward shift of the conductance–voltage relationship and that a single ILT-containing subunit is sufficient to induce a large enthalpic and entropic barrier, limiting opening of the intracellular gate.

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6

Castillo, Karen, Amaury Pupo, David Baez-Nieto, Gustavo F. Contreras, Francisco J. Morera, Alan Neely, Ramon Latorre, and Carlos Gonzalez. "Voltage-gated proton (Hv 1) channels, a singular voltage sensing domain." FEBS Letters 589, no. 22 (August 18, 2015): 3471–78. http://dx.doi.org/10.1016/j.febslet.2015.08.003.

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7

Bertz, Morten, and Kazuhiko Kinosita. "3PT166 Controlling an ion channel's voltage sensing domain without voltage(The 50th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 52, supplement (2012): S169. http://dx.doi.org/10.2142/biophys.52.s169_5.

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8

Fox, W. Everett, and Carlos A. Villalba-Galea. "S3-S4 Loop Modulates Voltage Sensing Domain Relaxation." Biophysical Journal 104, no. 2 (January 2013): 466a—467a. http://dx.doi.org/10.1016/j.bpj.2012.11.2579.

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9

Van Horn, Wade D., Parthasarathi Rath, and Nicholas Sisco. "Biophysical Characterization of the TRPM8 Voltage-Sensing Domain." Biophysical Journal 106, no. 2 (January 2014): 756a. http://dx.doi.org/10.1016/j.bpj.2013.11.4160.

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10

Zhao, Juan, and Rikard Blunck. "Mode Shift of Shaker Isolated-Voltage Sensing Domain." Biophysical Journal 114, no. 3 (February 2018): 546a. http://dx.doi.org/10.1016/j.bpj.2017.11.2982.

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11

Muroi, Yukiko, and Baron Chanda. "Local Anesthetics Disrupt Energetic Coupling between the Voltage-sensing Segments of a Sodium Channel." Journal of General Physiology 133, no. 1 (December 15, 2008): 1–15. http://dx.doi.org/10.1085/jgp.200810103.

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Local anesthetics block sodium channels in a state-dependent fashion, binding with higher affinity to open and/or inactivated states. Gating current measurements show that local anesthetics immobilize a fraction of the gating charge, suggesting that the movement of voltage sensors is modified when a local anesthetic binds to the pore of the sodium channel. Here, using voltage clamp fluorescence measurements, we provide a quantitative description of the effect of local anesthetics on the steady-state behavior of the voltage-sensing segments of a sodium channel. Lidocaine and QX-314 shifted the midpoints of the fluorescence–voltage (F-V) curves of S4 domain III in the hyperpolarizing direction by 57 and 65 mV, respectively. A single mutation in the S6 of domain IV (F1579A), a site critical for local anesthetic block, abolished the effect of QX-314 on the voltage sensor of domain III. Both local anesthetics modestly shifted the F-V relationships of S4 domain IV toward hyperpolarized potentials. In contrast, the F-V curve of the S4 domain I was shifted by 11 mV in the depolarizing direction upon QX-314 binding. These antagonistic effects of the local anesthetic indicate that the drug modifies the coupling between the voltage-sensing domains of the sodium channel. Our findings suggest a novel role of local anesthetics in modulating the gating apparatus of the sodium channel.

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12

Min Leong, Lee, Bok Eum Kang, and Bradley J. Baker. "A Voltage Dependent Heterotrimeric FRET Signal Suggests Multimeric Association for the Voltage Sensing Domain of the Voltage Sensing Phosphatase." Biophysical Journal 116, no. 3 (February 2019): 146a. http://dx.doi.org/10.1016/j.bpj.2018.11.811.

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13

Li, Qufei, Sherry Wanderling, Marcin Paduch, David Medovoy, Abhishek Singharoy, Ryan McGreevy, Carlos A. Villalba-Galea, et al. "Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain." Nature Structural & Molecular Biology 21, no. 3 (February 2, 2014): 244–52. http://dx.doi.org/10.1038/nsmb.2768.

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14

Li, Qufei, Sherry Wanderling, Marcin Paduch, David Medovoy, Carlos Villalba-Galea, Raymond Hulse, Benoit Roux, Anthony Kossiakoff, and Eduardo Perozo. "Structural Mechanism of Voltage-Dependent Gating in an Isolated Voltage-Sensing Domain." Biophysical Journal 104, no. 2 (January 2013): 196a. http://dx.doi.org/10.1016/j.bpj.2012.11.1108.

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15

Hong, Liang, Medha M. Pathak, Iris H. Kim, Dennis Ta, and Francesco Tombola. "Voltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains." Neuron 79, no. 1 (July 2013): 202. http://dx.doi.org/10.1016/j.neuron.2013.06.031.

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16

Hong, Liang, Medha M. Pathak, Iris H. Kim, Dennis Ta, and Francesco Tombola. "Voltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains." Neuron 77, no. 2 (January 2013): 274–87. http://dx.doi.org/10.1016/j.neuron.2012.11.013.

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17

Villalba-Galea, Carlos A., Ludivine Frezza, Walter Sandtner, and Francisco Bezanilla. "Sensing charges of the Ciona intestinalis voltage-sensing phosphatase." Journal of General Physiology 142, no. 5 (October 14, 2013): 543–55. http://dx.doi.org/10.1085/jgp.201310993.

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Voltage control over enzymatic activity in voltage-sensitive phosphatases (VSPs) is conferred by a voltage-sensing domain (VSD) located in the N terminus. These VSDs are constituted by four putative transmembrane segments (S1 to S4) resembling those found in voltage-gated ion channels. The putative fourth segment (S4) of the VSD contains positive residues that likely function as voltage-sensing elements. To study in detail how these residues sense the plasma membrane potential, we have focused on five arginines in the S4 segment of the Ciona intestinalis VSP (Ci-VSP). After implementing a histidine scan, here we show that four arginine-to-histidine mutants, namely R223H to R232H, mediate voltage-dependent proton translocation across the membrane, indicating that these residues transit through the hydrophobic core of Ci-VSP as a function of the membrane potential. These observations indicate that the charges carried by these residues are sensing charges. Furthermore, our results also show that the electrical field in VSPs is focused in a narrow hydrophobic region that separates the extracellular and intracellular space and constitutes the energy barrier for charge crossing.

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18

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 (October 29, 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, but several compounds have been shown to influence the voltage-sensing domain. An important unexplored feature of these compounds is the influence of channel gating on drug binding or effects. In the present study, we compare the state-dependent actions of retigabine and ICA-069673 (ICA73, a voltage sensor–targeted activator). We assess drug binding to preopen states by applying drugs to homomeric KCNQ2 channels at different holding voltages, demonstrating little or no association of ICA73 with resting states. Using rapid solution switching, we also demonstrate that the rate of onset of ICA73 correlates with the voltage dependence of channel activation. Retigabine actions differ significantly, with prominent drug effects seen at very negative holding voltages and distinct voltage dependences of drug binding versus channel activation. Using similar approaches, we investigate the mechanistic basis for attenuation of ICA73 actions by the voltage-sensing domain mutation KCNQ2[A181P]. Our findings demonstrate different state-dependent actions of pore- versus voltage sensor–targeted KCNQ channel activators, which highlight that subtypes of this drug class operate with distinct mechanisms.

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19

Schow, Eric V., Karun Gogna, J. Alfredo Freites, Douglas J. Tobias, and Stephen H. White. "Down-State Model of the KvAP Voltage-Sensing Domain." Biophysical Journal 96, no. 3 (February 2009): 484a. http://dx.doi.org/10.1016/j.bpj.2008.12.2497.

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20

Taylor, Keenan C., Georg Kuenze, Hui Huang, and Chuck R. Sanders. "NMR Structure of the Human KCNQ1 Voltage-Sensing Domain." Biophysical Journal 114, no. 3 (February 2018): 238a. http://dx.doi.org/10.1016/j.bpj.2017.11.1324.

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21

Loots, Eli, and Ehud Y. Isacoff. "Molecular Coupling of S4 to a K+ Channel's Slow Inactivation Gate." Journal of General Physiology 116, no. 5 (October 16, 2000): 623–36. http://dx.doi.org/10.1085/jgp.116.5.623.

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The mechanism by which physiological signals regulate the conformation of molecular gates that open and close ion channels is poorly understood. Voltage clamp fluorometry was used to ask how the voltage-sensing S4 transmembrane domain is coupled to the slow inactivation gate in the pore domain of the Shaker K+ channel. Fluorophores attached at several sites in S4 indicate that the voltage-sensing rearrangements are followed by an additional inactivation motion. Fluorophores attached at the perimeter of the pore domain indicate that the inactivation rearrangement projects from the selectivity filter out to the interface with the voltage-sensing domain. Some of the pore domain sites also sense activation, and this appears to be due to a direct interaction with S4 based on the finding that S4 comes into close enough proximity to the pore domain for a pore mutation to alter the nanoenvironment of an S4-attached fluorophore. We propose that activation produces an S4–pore domain interaction that disrupts a bond between the S4 contact site on the pore domain and the outer end of S6. Our results indicate that this bond holds the slow inactivation gate open and, therefore, we propose that this S4-induced bond disruption triggers inactivation.

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22

Rajakumar, Dhanarajan, Hong-hua Piao, Bok Eum Kang, Arong Jung, Eun Ha Kim, and Bradley J. Baker. "V220 Mutants of Ciona Voltage-Sensing Domain Based Genetically Encoded Fluorescent Voltage Sensors." Biophysical Journal 108, no. 2 (January 2015): 151a—152a. http://dx.doi.org/10.1016/j.bpj.2014.11.835.

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23

Li-Smerin, Yingying, David H. Hackos, and Kenton J. Swartz. "α-Helical Structural Elements within the Voltage-Sensing Domains of a K+ Channel." Journal of General Physiology 115, no. 1 (December 28, 1999): 33–50. http://dx.doi.org/10.1085/jgp.115.1.33.

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Voltage-gated K+ channels are tetramers with each subunit containing six (S1–S6) putative membrane spanning segments. The fifth through sixth transmembrane segments (S5–S6) from each of four subunits assemble to form a central pore domain. A growing body of evidence suggests that the first four segments (S1–S4) comprise a domain-like voltage-sensing structure. While the topology of this region is reasonably well defined, the secondary and tertiary structures of these transmembrane segments are not. To explore the secondary structure of the voltage-sensing domains, we used alanine-scanning mutagenesis through the region encompassing the first four transmembrane segments in the drk1 voltage-gated K+ channel. We examined the mutation-induced perturbation in gating free energy for periodicity characteristic of α-helices. Our results are consistent with at least portions of S1, S2, S3, and S4 adopting α-helical secondary structure. In addition, both the S1–S2 and S3–S4 linkers exhibited substantial helical character. The distribution of gating perturbations for S1 and S2 suggest that these two helices interact primarily with two environments. In contrast, the distribution of perturbations for S3 and S4 were more complex, suggesting that the latter two helices make more extensive protein contacts, possibly interfacing directly with the shell of the pore domain.

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24

Song, Weizhong, Yuzhe Du, Zhiqi Liu, Ningguang Luo, Michael Turkov, Dalia Gordon, Michael Gurevitz, Alan L. Goldin, and Ke Dong. "Substitutions in the Domain III Voltage-sensing Module Enhance the Sensitivity of an Insect Sodium Channel to a Scorpion β-Toxin." Journal of Biological Chemistry 286, no. 18 (March 15, 2011): 15781–88. http://dx.doi.org/10.1074/jbc.m110.217000.

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Scorpion β-toxins bind to the extracellular regions of the voltage-sensing module of domain II and to the pore module of domain III in voltage-gated sodium channels and enhance channel activation by trapping and stabilizing the voltage sensor of domain II in its activated state. We investigated the interaction of a highly potent insect-selective scorpion depressant β-toxin, Lqh-dprIT3, from Leiurus quinquestriatus hebraeus with insect sodium channels from Blattella germanica (BgNav). Like other scorpion β-toxins, Lqh-dprIT3 shifts the voltage dependence of activation of BgNav channels expressed in Xenopus oocytes to more negative membrane potentials but only after strong depolarizing prepulses. Notably, among 10 BgNav splice variants tested for their sensitivity to the toxin, only BgNav1-1 was hypersensitive due to an L1285P substitution in IIIS1 resulting from a U-to-C RNA-editing event. Furthermore, charge reversal of a negatively charged residue (E1290K) at the extracellular end of IIIS1 and the two innermost positively charged residues (R4E and R5E) in IIIS4 also increased the channel sensitivity to Lqh-dprIT3. Besides enhancement of toxin sensitivity, the R4E substitution caused an additional 20-mV negative shift in the voltage dependence of activation of toxin-modified channels, inducing a unique toxin-modified state. Our findings provide the first direct evidence for the involvement of the domain III voltage-sensing module in the action of scorpion β-toxins. This hypersensitivity most likely reflects an increase in IIS4 trapping via allosteric mechanisms, suggesting coupling between the voltage sensors in neighboring domains during channel activation.

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25

Flynn, Galen E., and William N. Zagotta. "Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels." Proceedings of the National Academy of Sciences 115, no. 34 (August 3, 2018): E8086—E8095. http://dx.doi.org/10.1073/pnas.1805596115.

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Hyperpolarization-activated, cyclic nucleotide-gated (HCN) ion channels are both voltage- and ligand-activated membrane proteins that contribute to electrical excitability and pace-making activity in cardiac and neuronal cells. These channels are members of the voltage-gated Kv channel superfamily and cyclic nucleotide-binding domain subfamily of ion channels. HCN channels have a unique feature that distinguishes them from other voltage-gated channels: the HCN channel pore opens in response to hyperpolarizing voltages instead of depolarizing voltages. In the canonical model of electromechanical coupling, based on Kv channels, a change in membrane voltage activates the voltage-sensing domains (VSD) and the activation energy passes to the pore domain (PD) through a covalent linker that connects the VSD to the PD. In this investigation, the covalent linkage between the VSD and PD, the S4-S5 linker, and nearby regions of spHCN channels were mutated to determine the functional role each plays in hyperpolarization-dependent activation. The results show that: (i) the S4-S5 linker is not required for hyperpolarization-dependent activation or ligand-dependent gating; (ii) the S4 C-terminal region (S4C-term) is not necessary for ligand-dependent gating but is required for hyperpolarization-dependent activation and acts like an autoinhibitory domain on the PD; (iii) the S5N-term region is involved in VSD–PD coupling and holding the pore closed; and (iv) spHCN channels have two voltage-dependent processes, a hyperpolarization-dependent activation and a depolarization-dependent recovery from inactivation. These results are inconsistent with the canonical model of VSD–PD coupling in Kv channels and elucidate the mechanism for hyperpolarization-dependent activation of HCN channels.

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26

Vargas, Ernesto, Carlos A. Villalba-Galea, Benoit Roux, and Francisco Bezanilla. "Structural Model of the Voltage Sensing Domain in Ci-VSP." Biophysical Journal 98, no. 3 (January 2010): 645a. http://dx.doi.org/10.1016/j.bpj.2009.12.3533.

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27

Schroder, Ryan V., Ping Wang, and Sebastien F. Poget. "Recombinant Expression of a Voltage Sensing Domain from Human NaV1.7." Biophysical Journal 114, no. 3 (February 2018): 633a. http://dx.doi.org/10.1016/j.bpj.2017.11.3421.

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28

Mishina, Yukiko, Hiroki Mutoh, and Thomas Knöpfel. "Transfer of Kv3.1 Voltage Sensor Features to the Isolated Ci-VSP Voltage-Sensing Domain." Biophysical Journal 103, no. 4 (August 2012): 669–76. http://dx.doi.org/10.1016/j.bpj.2012.07.031.

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29

Arrigoni, Cristina, Indra Schroeder, Giulia Romani, James L. Van Etten, Gerhard Thiel, and Anna Moroni. "The voltage-sensing domain of a phosphatase gates the pore of a potassium channel." Journal of General Physiology 141, no. 3 (February 25, 2013): 389–95. http://dx.doi.org/10.1085/jgp.201210940.

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The modular architecture of voltage-gated K+ (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channel Kcv creates KvSynth1, a functional voltage-gated, outwardly rectifying K+ channel. KvSynth1 displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V1/2 = +56 mV; z of ∼1), including the depolarization-induced mode shift. The degree of outward rectification of the channel is critically dependent on the length of the linker more than on its amino acid composition. This highlights a mechanistic role of the linker in transmitting the movement of the sensor to the pore and shows that electromechanical coupling can occur without coevolution of the two domains.

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30

Gonzalez, Carlos, Santiago Rebolledo, Marta E. Perez, and H. Peter Larsson. "Molecular mechanism of voltage sensing in voltage-gated proton channels." Journal of General Physiology 141, no. 3 (February 11, 2013): 275–85. http://dx.doi.org/10.1085/jgp.201210857.

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Voltage-gated proton (Hv) channels play an essential role in phagocytic cells by generating a hyperpolarizing proton current that electrically compensates for the depolarizing current generated by the NADPH oxidase during the respiratory burst, thereby ensuring a sustained production of reactive oxygen species by the NADPH oxidase in phagocytes to neutralize engulfed bacteria. Despite the importance of the voltage-dependent Hv current, it is at present unclear which residues in Hv channels are responsible for the voltage activation. Here we show that individual neutralizations of three charged residues in the fourth transmembrane domain, S4, all reduce the voltage dependence of activation. In addition, we show that the middle S4 charged residue moves from a position accessible from the cytosolic solution to a position accessible from the extracellular solution, suggesting that this residue moves across most of the membrane electric field during voltage activation of Hv channels. Our results show for the first time that the charge movement of these three S4 charges accounts for almost all of the measured gating charge in Hv channels.

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31

Hong, Liang, Iris Kim, Medha M. Pathak, Dennis Ta, and Francesco Tombola. "Hv1 Inhibitors Reveal Gating Properties Typical of Pore Domains in a Voltage-Sensing Domain." Biophysical Journal 102, no. 3 (January 2012): 685a—686a. http://dx.doi.org/10.1016/j.bpj.2011.11.3726.

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32

Sakata, Souhei, Tatsuki Kurokawa, Morten H. H. Nørholm, Masahiro Takagi, Yoshifumi Okochi, Gunnar von Heijne, and Yasushi Okamura. "Functionality of the voltage-gated proton channel truncated in S4." Proceedings of the National Academy of Sciences 107, no. 5 (December 14, 2009): 2313–18. http://dx.doi.org/10.1073/pnas.0911868107.

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The voltage sensor domain (VSD) is the key module for voltage sensing in voltage-gated ion channels and voltage-sensing phosphatases. Structurally, both the VSD and the recently discovered voltage-gated proton channels (Hv channels) voltage sensor only protein (VSOP) and Hv1 contain four transmembrane segments. The fourth transmembrane segment (S4) of Hv channels contains three periodically aligned arginines (R1, R2, R3). It remains unknown where protons permeate or how voltage sensing is coupled to ion permeation in Hv channels. Here we report that Hv channels truncated just downstream of R2 in the S4 segment retain most channel properties. Two assays, site-directed cysteine-scanning using accessibility of maleimide-reagent as detected by Western blotting and insertion into dog pancreas microsomes, both showed that S4 inserts into the membrane, even if it is truncated between the R2 and R3 positions. These findings provide important clues to the molecular mechanism underlying voltage sensing and proton permeation in Hv channels.

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33

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 (October 23, 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 closely overlap under basal PIP2 conditions. Retigabine stabilizes the conducting conformation of the pore and the activated voltage sensor conformation, leading to dramatic deceleration of current and fluorescence deactivation, but these effects are attenuated upon disruption of channel:PIP2 interactions. These findings reveal an important role for PIP2 in coupling retigabine binding to altered VSD function. We identify a polybasic motif in the proximal C terminus of retigabine-sensitive KCNQ channels that contributes to VSD–pore coupling via PIP2, and thereby influences the unique gating effects of retigabine.

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34

Yang, Junqiu, Huanghe Yang, Xiaohui Sun, Kelli Delaloye, Xiao Yang, Alyssa Moller, Jingyi Shi, and Jianmin Cui. "Interaction between residues in the Mg2+-binding site regulates BK channel activation." Journal of General Physiology 141, no. 2 (January 28, 2013): 217–28. http://dx.doi.org/10.1085/jgp.201210794.

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As a unique member of the voltage-gated potassium channel family, a large conductance, voltage- and Ca2+-activated K+ (BK) channel has a large cytosolic domain that serves as the Ca2+ sensor, in addition to a membrane-spanning domain that contains the voltage-sensing (VSD) and pore-gate domains. The conformational changes of the cytosolic domain induced by Ca2+ binding and the conformational changes of the VSD induced by membrane voltage changes trigger the opening of the pore-gate domain. Although some structural information of these individual functional domains is available, how the interactions among these domains, especially the noncovalent interactions, control the dynamic gating process of BK channels is still not clear. Previous studies discovered that intracellular Mg2+ binds to an interdomain binding site consisting of D99 and N172 from the membrane-spanning domain and E374 and E399 from the cytosolic domain. The bound Mg2+ at this narrow interdomain interface activates the BK channel through an electrostatic interaction with a positively charged residue in the VSD. In this study, we investigated the potential interdomain interactions between the Mg2+-coordination residues and their effects on channel gating. By introducing different charges to these residues, we discovered a native interdomain interaction between D99 and E374 that can affect BK channel activation. To understand the underlying mechanism of the interdomain interactions between the Mg2+-coordination residues, we introduced artificial electrostatic interactions between residues 172 and 399 from two different domains. We found that the interdomain interactions between these two positions not only alter the local conformations near the Mg2+-binding site but also change distant conformations including the pore-gate domain, thereby affecting the voltage- and Ca2+-dependent activation of the BK channel. These results illustrate the importance of interdomain interactions to the allosteric gating mechanisms of BK channels.

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35

Kariev, Alisher M., and Michael E. Green. "Quantum Calculations of Large Segments of a Voltage Sensing Domain of a Voltage Gated Channel." Biophysical Journal 112, no. 3 (February 2017): 543a. http://dx.doi.org/10.1016/j.bpj.2016.11.2934.

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36

Sedwick, Caitlin. "Gating ring strengthens marriage of BK channel voltage sensing to pore opening." Journal of General Physiology 149, no. 3 (February 15, 2017): 295. http://dx.doi.org/10.1085/jgp.201711768.

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37

Nakajo, Koichi, and Yoshihiro Kubo. "KCNQ1 channel modulation by KCNE proteins via the voltage-sensing domain." Journal of Physiology 593, no. 12 (February 16, 2015): 2617–25. http://dx.doi.org/10.1113/jphysiol.2014.287672.

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38

Tombola, Francesco, Medha M. Pathak, Pau Gorostiza, and Ehud Y. Isacoff. "The twisted ion-permeation pathway of a resting voltage-sensing domain." Nature 445, no. 7127 (December 24, 2006): 546–49. http://dx.doi.org/10.1038/nature05396.

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39

Taylor, Keenan C., Hui Huang, and Charles R. Sanders. "Structural Characterization of the Human KCNQ1 Voltage-Sensing Domain by NMR." Biophysical Journal 112, no. 3 (February 2017): 502a. http://dx.doi.org/10.1016/j.bpj.2016.11.2717.

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40

Keer, Harindar S., J. Alfredo Freites, Stephen H. White, and Douglas J. Tobias. "A potassium Channel Voltage-Sensing Domain in a Non-Phospholipid Bilayer." Biophysical Journal 100, no. 3 (February 2011): 282a. http://dx.doi.org/10.1016/j.bpj.2010.12.1747.

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41

Palovcak, Eugene, and Vincenzo Carnevale. "Correlating Residue Coevolution and Function in a Conserved Voltage-Sensing Domain." Biophysical Journal 104, no. 2 (January 2013): 277a. http://dx.doi.org/10.1016/j.bpj.2012.11.1553.

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42

Zolman, Kevin D., Paul M. Castle, and Susy C. Kohout. "The Role of the C2 Domain of Voltage Sensing Phosphatase (VSP)." Biophysical Journal 108, no. 2 (January 2015): 425a. http://dx.doi.org/10.1016/j.bpj.2014.11.2327.

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43

Zhao, Juan, and Rikard Blunck. "Role of the Voltage Sensing Domain S1-S4 in TRPV1 Channels." Biophysical Journal 108, no. 2 (January 2015): 427a. http://dx.doi.org/10.1016/j.bpj.2014.11.2337.

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44

DeCoursey, Thomas E. "Voltage-Gated Proton Channels Find Their Dream Job Managing the Respiratory Burst in Phagocytes." Physiology 25, no. 1 (February 2010): 27–40. http://dx.doi.org/10.1152/physiol.00039.2009.

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Abstract:

The voltage-gated proton channel bears surprising resemblance to the voltage-sensing domain (S1–S4) of other voltage-gated ion channels but is a dimer with two conduction pathways. The proton channel seems designed for efficient proton extrusion from cells. In phagocytes, it facilitates the production of reactive oxygen species by NADPH oxidase.

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45

Mishima, Eriko, Yoko Sato, Kei Nanatani, Naomi Hoshi, Jong-Kook Lee, Nina Schiller, Gunnar von Heijne, Masao Sakaguchi, and Nobuyuki Uozumi. "The topogenic function of S4 promotes membrane insertion of the voltage-sensor domain in the KvAP channel." Biochemical Journal 473, no. 23 (November 25, 2016): 4361–72. http://dx.doi.org/10.1042/bcj20160746.

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Voltage-dependent K+ (KV) channels control K+ permeability in response to shifts in the membrane potential. Voltage sensing in KV channels is mediated by the positively charged transmembrane domain S4. The best-characterized KV channel, KvAP, lacks the distinct hydrophilic region corresponding to the S3–S4 extracellular loop that is found in other K+ channels. In the present study, we evaluated the topogenic properties of the transmembrane regions within the voltage-sensing domain in KvAP. S3 had low membrane insertion activity, whereas S4 possessed a unique type-I signal anchor (SA-I) function, which enabled it to insert into the membrane by itself. S4 was also found to function as a stop-transfer signal for retention in the membrane. The length and structural nature of the extracellular S3–S4 loop affected the membrane insertion of S3 and S4, suggesting that S3 membrane insertion was dependent on S4. Replacement of charged residues within the transmembrane regions with residues of opposite charge revealed that Asp72 in S2 and Glu93 in S3 contributed to membrane insertion of S3 and S4, and increased the stability of S4 in the membrane. These results indicate that the SA-I function of S4, unique among K+ channels studied to date, promotes the insertion of S3 into the membrane, and that the charged residues essential for voltage sensing contribute to the membrane-insertion of the voltage sensor domain in KvAP.

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Shimomura, Takushi, and Yoshihiro Kubo. "Phosphoinositides modulate the voltage dependence of two-pore channel 3." Journal of General Physiology 151, no. 8 (June 10, 2019): 986–1006. http://dx.doi.org/10.1085/jgp.201812285.

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Two-pore channels, or two-pore Na+ channels (TPCs), contain two homologous domains, each containing a functional unit typical of voltage-dependent cation channels. Each domain is considered to be responsible for either phosphoinositide (PI) binding or voltage sensing. Among the three members of the TPC family, TPC1 and TPC2 are activated by PI(3,5)P2, while TPC3 has been thought not to be affected by any PIs. Here, we report that TPC3 is sensitive to PI(3,4)P2 and PI(3,5)P2, but not to PI(4,5)P2, and that the extremely slow increase in TPC3 currents induced by depolarization in Xenopus oocytes is due to the production of PI(3,4)P2. Similarly to TPC1, the cluster of basic amino acid residues in domain I is critical for PI sensitivity, but with a slight variation that may allow TPC3 to be sensitive to both PI(3,4)P2 and PI(3,5)P2. We also found that TPC3 has a unique PI-dependent modulation mechanism of voltage dependence, which is achieved by a specific bridging interaction between domain I and domain II. Taken together, these findings show that TPC3 is a unique member of the TPC family that senses PIs and displays a strong coupling between PI binding and voltage-dependent gating.

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Kasimova, Marina A., Erik Lindahl, and Lucie Delemotte. "Determining the molecular basis of voltage sensitivity in membrane proteins." Journal of General Physiology 150, no. 10 (August 27, 2018): 1444–58. http://dx.doi.org/10.1085/jgp.201812086.

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Voltage-sensitive membrane proteins are united by their ability to transform changes in membrane potential into mechanical work. They are responsible for a spectrum of physiological processes in living organisms, including electrical signaling and cell-cycle progression. Although the mechanism of voltage-sensing has been well characterized for some membrane proteins, including voltage-gated ion channels, even the location of the voltage-sensing elements remains unknown for others. Moreover, the detection of these elements by using experimental techniques is challenging because of the diversity of membrane proteins. Here, we provide a computational approach to predict voltage-sensing elements in any membrane protein, independent of its structure or function. It relies on an estimation of the propensity of a protein to respond to changes in membrane potential. We first show that this property correlates well with voltage sensitivity by applying our approach to a set of voltage-sensitive and voltage-insensitive membrane proteins. We further show that it correctly identifies authentic voltage-sensitive residues in the voltage-sensor domain of voltage-gated ion channels. Finally, we investigate six membrane proteins for which the voltage-sensing elements have not yet been characterized and identify residues and ions that might be involved in the response to voltage. The suggested approach is fast and simple and enables a characterization of voltage sensitivity that goes beyond mere identification of charges. We anticipate that its application before mutagenesis experiments will significantly reduce the number of potential voltage-sensitive elements to be tested.

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Milescu, Mirela, Hwa C. Lee, Chan Hyung Bae, Jae Il Kim, and Kenton J. Swartz. "Opening the Shaker K+ channel with hanatoxin." Journal of General Physiology 141, no. 2 (January 28, 2013): 203–16. http://dx.doi.org/10.1085/jgp.201210914.

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Voltage-activated ion channels open and close in response to changes in membrane voltage, a property that is fundamental to the roles of these channels in electrical signaling. Protein toxins from venomous organisms commonly target the S1–S4 voltage-sensing domains in these channels and modify their gating properties. Studies on the interaction of hanatoxin with the Kv2.1 channel show that this tarantula toxin interacts with the S1–S4 domain and inhibits opening by stabilizing a closed state. Here we investigated the interaction of hanatoxin with the Shaker Kv channel, a voltage-activated channel that has been extensively studied with biophysical approaches. In contrast to what is observed in the Kv2.1 channel, we find that hanatoxin shifts the conductance–voltage relation to negative voltages, making it easier to open the channel with membrane depolarization. Although these actions of the toxin are subtle in the wild-type channel, strengthening the toxin–channel interaction with mutations in the S3b helix of the S1-S4 domain enhances toxin affinity and causes large shifts in the conductance–voltage relationship. Using a range of previously characterized mutants of the Shaker Kv channel, we find that hanatoxin stabilizes an activated conformation of the voltage sensors, in addition to promoting opening through an effect on the final opening transition. Chimeras in which S3b–S4 paddle motifs are transferred between Kv2.1 and Shaker Kv channels, as well as experiments with the related tarantula toxin GxTx-1E, lead us to conclude that the actions of tarantula toxins are not simply a product of where they bind to the channel, but that fine structural details of the toxin–channel interface determine whether a toxin is an inhibitor or opener.

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Liu, Guoxia, Xiaowei Niu, Roland S. Wu, Neelesh Chudasama, Yongneng Yao, Xin Jin, Richard Weinberg, et al. "Location of modulatory β subunits in BK potassium channels." Journal of General Physiology 135, no. 5 (April 12, 2010): 449–59. http://dx.doi.org/10.1085/jgp.201010417.

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Large-conductance voltage- and calcium-activated potassium (BK) channels contain four pore-forming α subunits and four modulatory β subunits. From the extents of disulfide cross-linking in channels on the cell surface between cysteine (Cys) substituted for residues in the first turns in the membrane of the S0 transmembrane (TM) helix, unique to BK α, and of the voltage-sensing domain TM helices S1–S4, we infer that S0 is next to S3 and S4, but not to S1 and S2. Furthermore, of the two β1 TM helices, TM2 is next to S0, and TM1 is next to TM2. Coexpression of α with two substituted Cys’s, one in S0 and one in S2, and β1 also with two substituted Cys’s, one in TM1 and one in TM2, resulted in two αs cross-linked by one β. Thus, each β lies between and can interact with the voltage-sensing domains of two adjacent α subunits.

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50

Hossain, Md Israil, Hirohide Iwasaki, Yoshifumi Okochi, Mohamed Chahine, Shinichi Higashijima, Kuniaki Nagayama, and Yasushi Okamura. "Enzyme Domain Affects the Movement of the Voltage Sensor in Ascidian and Zebrafish Voltage-sensing Phosphatases." Journal of Biological Chemistry 283, no. 26 (March 28, 2008): 18248–59. http://dx.doi.org/10.1074/jbc.m706184200.

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