IndraLab

Statements

MINK1 binds KCNQ1. 19 / 19
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"To modulate gating and current amplitude, MinK presumably must associate with KvLQT1 in a specific manner."
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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"Finally, for modulation to occur, MinK must presumably associate with KvLQT1, but it was previously unknown whether this involves the same or different structures responsible for the gating and current amplitude effects."
10962015
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"Thus, KVLQT1 interacts with minK to form the cardiac slowly activating, delayed rectifier I Ks current."
9791861
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"These results suggested that SCN5A mutations act through a gain-of-function mechanism (the mutant channel functions normally, but with altered properties) and that the mechanism of chromosome-3-linked[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
9791861
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"8,9 The minK and KvLQT1 complex channel is responsible for the slowly activating component of the delayed rectifier K + channel (I Ks channel), and I Ks is important for the repolarization of cardiac [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
11697903
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"Gating of the delayed rectifier K+ channel KvLQT1 is drastically slowed by the association with the small membrane protein minK and it is thought that the KvLQT1 and minK complex underlies the slow delayed rectifier K+ current of cardiac cells."
9817805
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"There is controversy about the effects of the association between KvLQT1 and minK on the single-channel conductance."
9817805
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"With the cloning of KVLQT1 and coexpression of KVLQT1 and minK in both mammalian cell lines and Xenopus oocytes, it became clear that KVLQT1 interacts with minK to form the cardiac slowly activating delayed-rectifier IKs current (47,48); minK alone can not form a functional channel but induces the IKs current by interacting with endogenous KVLQT1 protein in Xenopus oocytes and mammalian cells."
11286954
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"Here we show that the KCNQ1 and minK interaction is influenced by the expression system."
11680622
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"This article reviews some of the recent work addressing the prototypical KCNE-channel interaction between minK and KvLQT1."
12069759
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"The presence and co-assembly of KvLQT1 and MinK in mouse brain (XREF_FIG) suggests that the protein may modulate neuronal excitability as a KvLQT1 and MinK complex as I KS does in heart."
20368164
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"A second current in this type is the, I Ks component mediated by heteromeric channel formed by Kv7.1 and MINK subunit protein that are encoded by KCNQ1 and KCNE1 genes, respectively."
25185978
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"10 Thus, minK interacts with both KCNQ1 and HERG, and KCNE1-3 proteins interact with Kv3.1 and Kv3.2 causing diversification of channel gating."
18313602
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"It is already known, for example, that minK can interact with KVLQT1 and HERG when overexpressed in heterologeous systems (McDonald et al., 1997)."
11239413
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"KvLQT1 and minK associate to form the functional slowly activated delayed rectifier potassium channel (I Ks) [12,13] while HERG and MiRP1 associate to form the rapidly activated delayed rectifier pota[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12051962
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"Because KvLQT1 subunits give rise to functional potassium channels when expressed alone, it is interesting to consider the nature of the interaction between minK and KvLQT1 that produces larger and more slowly activating currents when these genes are coexpressed."
9834139
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"These efforts have left many unanswered questions regarding how MinK interacts with KvLQT1."
10962015
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"While MinK and KvLQT1 complexes recreate the behaviors of I Ks channels, MiRP1 and HERG complexes recapitulate those of I Kr channels."
10219239