IndraLab

Statements


KCNQ1 binds KCNE. 6 / 6
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"1 The channel associates with KCNE beta subunits that enforce prominent changes in the KCNQ1 (minK) current kinetics, which is likely one of the reasons for KCNQ1 and KCNE complexes being capable of p[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Activation of ATP sensitive P2Y4 receptors leads to phosphorylation and de-activation of the KCNQ1 and KCNE complex, thus decreasing potassium secretion into scala media and consequently lowering the hair cell sensory transduction driving force."

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"In light of the structural studies that KCNE3 imposes a counterclockwise rotation of the whole VSD relative to the PD of KCNQ1 channels and functional studies that KCNE1 most likely shares a similar location with KCNE3 in the KCNQ1/KCNE complex , we propose that KCNE1 rotates the VSD towards to the PD of KCNQ1."

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"The allosteric gating features, from this point of view, open what we believe to be a new perspective for reevaluation of KCNQ1 and KCNE complex regulation both in heterologous expression systems and [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Further, we show that the external K+ sensitivity of the heteromeric KCNQ1/KCNE complexes depends on the type of associated KCNE subunits."

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"While for neither protein does the N-terminus appear to be critical for dictating the channel-modulatory properties, the N-terminus is known to affect the pH sensitivity and pharmacological properties of the assembled KCNE and KCNQ1 complex."