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Pyraclofos activates KCNQ1. 35 / 35
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"However, after application of CP1 via injection into the oocyte, the KCNQ1 currents increased with consecutive voltage pulses, and current kinetics showed no declination during each pulse (10 µM CP1, Fig. 2a, b), indicating that CP1 permits voltage-dependent activation of KCNQ1 channels, despite the depletion of PIP ."
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"During a depolarizing voltage pulse that activates KCNQ1 channels, a fast decaying current following a brief hyperpolarization has been typically viewed as evidence of KCNQ1 channel inactivation."
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"Angelo and colleagues (2002) recently showed that MiRP4 ( KCNE5 ) shifts both time- and voltage-dependent modulation of KCNQ1 in the same direction as that achieved by MinK but to a much greater exten[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As shown in Fig. xref , paroxetine caused a slight rightward shift in the voltage-dependent activation of Kv7.1 with its V 1/2 shifted to a more depolarized potential at 4.6 ± 2.1 mV from −3.2 ± 2.1 mV ( n  = 7)."
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"CP1 modifies voltage-dependent activation of KCNQ1 channels by shifting the voltage dependence of channel opening, measured as the voltage dependence of the conductance (G–V) relationship, to more negative voltages (Fig. 1c) among other characteristics (see below)."
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"The voltage-activated K + channel Kv7.1, previously called KvLQT1, is expressed in several tissues, including the heart, kidney and cells in the inner ear lateral wall."
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"XREF_BIBR The KCNQ1 gene codifies KVLQT1 (Kv7.1), a voltage activated potassium channel alpha-subunit expressed in various cell types, including cardiac myocytes."
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"KCNQ1 and KCNE1 Channel Activation by Voltage."
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"We analyzed ML277-induced changes in the voltage-dependent activation of KCNQ1 channels."
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"In this brief review we will discuss the current evidence regarding the mechanism by which KCNE1 regulates the voltage dependent activation of KCNQ1 as the best understood example of KCNE regulation of K V channel gating."
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"A subsequent voltage pulse elicited much smaller KCNQ1 currents (Rundown trace, Fig. 2a) as a result of PIP depletion that had insufficient time to be replenished by endogenous enzymes between the pulses."
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"While the voltage dependent activation of KCNQ1 and the concatamer remained constant over time, it showed a time-dependent change throughout the 14 days expression period for KCNQ1+KCNE1 ( Fig. 2 B)."
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"These results suggest that CP1 facilitates voltage-dependent activation of KCNQ1 by favoring pore opening at various voltages."
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"These results suggest the idea that CP1 interacts with the channel, such that pore opening is enhanced even in the absence of VSD activation, and that it mediates VSD-pore coupling during voltage-dependent activation in KCNQ1 channels."
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"Additionally, to test the second hypothesis that all four voltage sensors need to activate to open KCNQ1 and KCNE1 channels, we used the mutation R231C that is assumed to lock the voltage sensor in the activated state [XREF_BIBR]."
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"These structural models do not identify the likely mechanism for how KCNE1 modulates the voltage dependent activation of KCNQ1 as the interactions with the VSD, PGD, and S4/S5 linker suggest that regulation of VSD movement, PGD opening, and electromechanical coupling are all plausible."
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"CP1 modifies voltage-dependent activation of KCNQ1 channels by shifting the voltage dependence of channel opening, measured as the voltage dependence of the conductance ( G – V ) relationship, to more negative voltages (Fig.  xref ) among other characteristics (see below)."
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"Together our findings suggest that altered charge-pair interactions within the voltage sensor module of KCNQ1 subunits may account for slowed I (Ks) deactivation induced by S140 or V141."
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"Determination and validation of the KCNQ1 VSD structures in the intermediate and activated states furnishes critical information for understanding the voltage-dependent activation of KCNQ1 and interactions with KCNE accessory subunits."
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"In summary, our study demonstrates that KCNE1 alters the kinetics and voltage dependence of voltage sensor activation and channel opening of KCNQ1 channels."
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"Roderick Mackinnon and his colleagues further analyzed the molecular basis for this special voltage activation of KCNQ1 [ 60 ]."
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"Phe applications strongly facilitated voltage dependent activation of KCNQ1 and KCNE1 channels (= ~ -20 mV in V 1/2) and increased the maximal conductance over 2-fold compared to the current with no Phe application (XREF_FIG)."
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"We also examined the effect of paroxetine on the voltage-dependent activation of Kv7.1, Kv7.4 and Kv7.5 channels at the concentrations near their IC values."
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"The current study found that SMIT1 regulates the effects of KCNE1 (and KCNE3) on KCNQ1 voltage activation, suggesting that SMIT1 and KCNE1 can form a macromolecular complex with KCNQ1."
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"As shown in Fig. 6A, paroxetine caused a slight rightward shift in the voltage-dependent activation of Kv7.1 with its V shifted to a more depolarized potential at 4.6 ± 2.1 mV from −3.2 ± 2.1 mV (n = 7)."
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"Voltage sensor activation should not be confused with voltage-dependent activation of the channel, which is a term historically used to describe channel opening in response to voltage changes, encompa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, after application of CP1 via injection into the oocyte, the KCNQ1 currents increased with consecutive voltage pulses, and current kinetics showed no declination during each pulse (10 µM CP1, Fig.  xref ), indicating that CP1 permits voltage-dependent activation of KCNQ1 channels, despite the depletion of PIP 2 ."
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"KCNE3 acts by promoting voltage sensor activation in KCNQ1."
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"In addition, it has been shown that voltage sensor activation in KCNQ1 proceeds through an intermediate step before reaching full activation XREF_BIBR."
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"We then also analyzed ML277-induced changes in the voltage-dependent activation of the KCNQ1 channel."
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"While the voltage dependent activation of KCNQ1 and the concatamer remained constant over time, it showed a time-dependent change throughout the 14 days expression period for KCNQ1+KCNE1 ( Fig. 2 B)."
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"In a study of channels with different numbers of the KCNQ1 subunit that contained a mutation in the voltage sensor, the results suggested that the voltage sensor in each subunit of both the KCNQ1 and [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As shown in Fig. 6B summarizing the voltage-dependent activation of KCNQ1-mediated currents, the amplitude of the mutant KCNQ1-mediated currents was significantly smaller than that of the WT currents.3.6 Effects of isoproterenol on AP properties of LQT1 iPSCs-derived cardiomyocytes."
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"C28 is another KCNQ1 activator molecule but binds to and stabilizes the voltage sensor domain, thereby decreasing the voltage required for voltage-dependent KCNQ1 activation (Lin et al., xref )."
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"We also examined the effect of paroxetine on the voltage-dependent activation of Kv7.1, Kv7.4 and Kv7.5 channels at the concentrations near their IC 50 values."
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