IndraLab

Statements

KCNQ1 inhibits Lys-Ser. 13 / 13
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"Finally, elimination of KCNQ1 slow inactivation by KCNE1 may also better enable I Ks to sustain rapid heart rates without current diminishment.The non inactivating status endowed by KCNE1 may also fac[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26410412
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"Heterologous expression studies demonstrated that mutations in KVLQT1 reduce I (Ks) by causing loss of channel function, altered channel gating, and/or a dominant negative effect."
10868746
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"For example, LQTS type I is caused by loss of function mutations in KvLQT1 that reduce the I Ks during AP repolarization."
26009542
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"The subunits KCNQ1 and KCNE1 generate the slowly activating, delayed rectifier potassium current, I Ks, that responds to sympathetic stimulation and is critical for human cardiac repolarization."
31461851
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"As shown in Figure 3A, coexpression of KCNQ1 -WT (0.5 mug) with KCNE1 (0.5 mug) produced a slowly activating outward WT-I Ks on depolarization to 30 mV from the holding potential of -80 mV."
24096004
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"Pathogenic variations in KCNQ1 reduce I Ks, prolonging the repolarization phase of the AP [XREF_BIBR, XREF_BIBR]."
28146053
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"LQT1 related mutations in KCNQ1 can impair the I Ks channel function by a number of mechanisms : (a) trafficking defects, (b) lower PIP 2 binding affinity, (c) reduced responsiveness to beta-adrenergic stimulation, and (d) gating kinetic defects."
25460172
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"An overexpression of miR-1/133 abolished KCNE1 and KCNQ1 expression, thus reducing the I KS with enhanced risk of lethal arrhythmias."
29259974
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"Finally, elimination of KCNQ1 slow inactivation by KCNE1 may also better enable I Ks to sustain rapid heart rates without current diminishment."
26410412
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"Co-expression of KCNE1 and wild-type KCNQ1 subunits in combination with KCNQ1-P343S subunits reduces I Ks currents by = ~ 60%."
15511625
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"In summary, in response to sustained beta-AR stimulation, CaMKII phosphorylates KCNQ1 at S484 to inhibit I Ks function."
29410121
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"In addition to inducing I Ks dysfunction through dominant negative loss-of-function effects and defective channel trafficking, mutations in KCNQ1 suppress I Ks channel function by reducing the channel affinity of interacting proteins XREF_BIBR, XREF_BIBR."
27761162
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"The founder of this family, KCNE1, also known as MinK (minimal K + channel protein), or IsK, was first found to co-assemble with the Kv alpha subunit Kv7.1 (KCNQ1) to form the slowly activating cardiac ventricular repolarization current I Ks."
22754540