Corpus ID: 27399725

Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel.

  title={Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel.},
  author={M. Sanguinetti and M. Curran and A. Zou and J. Shen and P. Spector and D. Atkinson and M. Keating},
  volume={384 6604},
The slowly activating delayed-rectifier K+ current, I(Ks), modulates the repolarization of cardiac action potentials. The molecular structure of the I(Ks) channel is not known, but physiological data indicate that one component of the I(Ks), channel is minK, a 130-amino-acid protein with a single putative transmembrane domain. The size and structure of this protein is such that it is unlikely that minK alone forms functional channels. We have previously used positional cloning techniques to… Expand
D242N, a K V 7.1 LQTS Mutation Uncovers a KEY Residue for I KS Voltage Dependence
Functional and computational analysis suggest that the clinical phenotype of the LQTS patients carrying the D242N mutation is due to impaired action potential adaptation to exercise and, in particular, to increase in heart rate. Expand
Structural and Functional Studies of the KCNQ1-KCNE K + Channel Complex: A Dissertation
KCNQ1 is a homotetrameric voltage-gated potassium channel expressed in cardiomyocytes and epithelial tissues. However, currents arising from KCNQ1 have never been physiologically observed. KCNQ1 isExpand
Mechanisms of I(Ks) suppression in LQT1 mutants.
This work examined for the first time trafficking of KvLQT1 mutations and correlated the results with the I(Ks) currents that were expressed and found a poor correlation for the severely dysfunctional mutations. Expand
Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel.
Docking to open KCNQ1 indicates that the extracellular end of the KCNE1 TMD forms an interface with an intersubunit cleft in the channel that is associated with most known gain-of-function disease mutations. Expand
Tea+-Sensitive Kcnq1 Constructs Reveal Pore-Independent Access to Kcne1 in Assembled I Ks Channels
Data strongly suggest that access of Cd2+ to the cysteine-mutated site on KCNE1 is independent of pore occlusion caused by TEA+ binding to the outer region of theKCNE1/V319Y pore, and that KC NE1 does not reside within the pore regions of the assembled channels. Expand
MinK-Related Peptide 1 Associates With Kv4.2 and Modulates Its Gating Function: Potential Role as &bgr; Subunit of Cardiac Transient Outward Channel?
  • Mei Zhang, Min Jiang, G. Tseng
  • Biology, Medicine
  • Circulation research
  • 2001
The data suggest that MiRP1 may serve as a regulatory subunit of Ito channels in the heart, supported by the observation thatMiRP1 induced an “overshoot” of Kv4.2 current amplitude during channel recovery from inactivation, similar to the overshoot of Ita described for human epicardial myocytes. Expand
Regulation of Kv4.3 Current by KChIP2 Splice Variants: A Component of Native Cardiac Ito?
A family of KChIP2 proteins is expressed in human hearts that exhibits differential modulation of hKv4.3 current in a Ca2+-dependent fashion and the absence of a gradient of protein across the ventricular wall suggest that K ChIP2 is either not a requisite component of human or canine ventricular Ito or that its functional effect is being affected or additionally modified by other factors present in myocardial cells. Expand
Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel
The competition of PIP2 and the calcified form of the calmodulin N lobe to a previously unidentified site in helix B of the proximal Kv7.1 C terminus is revealed, revealing a critical site where CaM competes with PIP1 to stabilize the channel open state. Expand
Regulation of the Kv2.1 Potassium Channel by MinK and MiRP1
Coimmunoprecipitations from rat heart tissue suggested that both MinK and MiRP1 form native cardiac complexes with Kv2.1 and support the possibility that inherited mutations in either subunit could contribute to cardiac arrhythmia by multiple mechanisms. Expand
The cardiac IKs channel, complex indeed
The cardiac IKs channel is a major repolarization current in the heart that responds rapidly and robustly to sympathetic nervous system stimulation to ensure adequate diastolic filling time in theExpand