IndraLab

Statements

CALM inhibits KCNQ1. 9 / 9
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"Given the numerous CaM variants exhibiting WT-like interaction with KCNQ1, some of the CaM variants may disrupt KCNQ1 baseline function leading to arrhythmogenesis observed in variant carriers."
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"By contrast, recent studies showing that KCNQ1 and I KS (KCNQ1/KCNE1) currents are stimulated by increases in intracellular Ca 2+ and are markedly inhibited by calmodulin antagonists [15] ."
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"Coexpression of CaM in Chinese hamster ovary (CHO) cells strongly reduced currents of KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3."
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"It has been suggested that CaM and Ca relieve KCNQ1 channel inactivation [4]."
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"Given the key role of KCNQ1 in the fight-or-flight response, CaM variants that perturb KCNQ1 function (e.g."
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"The slowly activating potassium current IKs was shown to be increased by elevation of Ca i , as due to a relief of KCNQ1 inactivation by calmodulin in a Ca 2+ dependent way (Ghosh et al., xref )."
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"Phosphatidylinositol 4,5 - bisphosphate ( PIP2 ) and Ca 2 + - calmodulin prevented Kv7.1 inactivation triggered by Ca 2 + - free external solutions , where Ser 182 at the S2-S3 linker relays the calmodulin signal from its inner boundary to the external pore to allow proper channel conduction ."
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"Moreover, overexpression of CaM reduced current amplitudes of KCNQ2, KCNQ4, and KCNQ5, but not those of KCNQ1 and KCNQ3."
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"As CaM N54I, A103V, D132H, D132N, and E141G exhibited similar binding affinity to KCNQ1 compared with CaM WT (Fig. 2C), the trafficking assay data indicate that these variants likely do not contribute to arrhythmia by modifying I or KCNQ1 current amplitude through changing channel trafficking efficiency.On the other hand, we found three CaM variants (E46K, F90L, and D132E) that reduced KCNQ1 trafficking efficiency compared with CaM WT (Fig. 3B and C and Table S3)."
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