IndraLab

Statements

MINK1 activates KCNQ1. 18 / 18
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"Previous data suggests that the ability of MinK to modulate KvLQT1 resides in amino acid residues 67-93 (Takumi et al. 1991; Ben-Efraim et al. 1996)."
10962015
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"A MinK and MiRP1 Chimera Modulates KvLQT1."
10962015
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"MinK modulates KvLQT1 gating by slowing activation and removing inactivation."
10962015
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"Despite the fact that MinK increases KCNQ1 unitary and macroscopic conductance ~ 4-fold, MinK knockout increased I K current in atrial myocytes; interestingly, this was not exclusively due to upregulation of currents sensitive to chromanol 293, a KCNQ1 and I Ks blocker."
19219384
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"Whether MinK mediated KvLQT1 association and modulation involves one or many MinK subregions is unknown."
10962015
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"The mechanism by which MinK modulates KvLQT1 gating is currently unknown."
10962015
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"Based on our previous results that indicate the MinK COOH terminus can modulate KvLQT1 only when an interaction between KvLQT1 and the MinK transmembrane domain occurs, we conclude that MiRP1 does not modulate KvLQT1; in part because of differences in the transmembrane domain that mediate KvLQT1 association."
10962015
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"In addition, a mutation in the MinK transmembrane domain associated with long QT syndrome has been found to alter MinK mediated KvLQT1 gating modulation (see below)."
10962015
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"In particular, we and others found that F340 is required for MinK modulation of KCNQ1 activation via MinK T58, and that an F340W mutation uncouples MinK-KCNQ1 (I Ks) channel activation from voltage, f[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
18567635
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"These studies indicate that, as in KVLQT1, mutations in minK can cause both autosomal dominant (Romano-Ward syndrome) and autosomal-recessive (JLN) LQT.Identification of SCN5A, HERG, KVLQT1 and minK a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
9791861
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"Our experiments using MinK and beta1 chimeras lacking a complete MinK transmembrane domain demonstrate that the MinK COOH terminus does not modulate KvLQT1 in the absence of the MinK transmembrane domain, even though the subdomains reach the plasma membrane."
10962015
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"Understanding how MinK associates with KvLQT1 and identifying subregions involved in gating modulation may provide insight into the mechanism by which MinK modulates KvLQT1."
10962015
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"MinK, a 129 amino acid protein containing one transmembrane spanning domain modulates KvLQT1, greatly slowing activation, increasing current amplitude, and removing inactivation."
10962015
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"To determine whether the MinK COOH terminus alone is sufficient to modulate KvLQT1, a chimera encoding the beta1 NH 2 terminus and transmembrane domain (amino acid residues 1-182) fused to the MinK COOH terminus (amino acid residues 67-129, beta1 and MinK1) was coexpressed in Xenopus oocytes with KvLQT1."
10962015
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"This conclusion supports the idea that two MinK subregions mediate association and modulation of KvLQT1."
10962015
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"MinK also modulates KvLQT1 current amplitude by an unknown mechanism that may or may not be dependent on gating."
10962015
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"MinK dramatically modulates KvLQT1 gating, slowing activation (XREF_FIG A, right), removing inactivation (B, right), and shifting the voltage dependence of activation to more positive potentials (D)."
10962015
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"Further, the formation of MinK-Kv2.1 complexes in vivo could explain the recent findings that kcne1 null mice exhibit atrial fibrillation, and that these mice show increased atrial myocyte I K compared to wild-type, a result inconsistent with effects on I Ks because MinK upregulates KCNQ1 current."
19219384