The MinK-related peptides

@article{McCrossan2004TheMP,
  title={The MinK-related peptides},
  author={Zoe A. McCrossan and Geoffrey W. Abbott},
  journal={Neuropharmacology},
  year={2004},
  volume={47},
  pages={787-821}
}
Pharmacological Approaches for the Modulation of the Potassium Channel KV4.x and KChIPs
Ion channels are macromolecular complexes present in the plasma membrane and intracellular organelles of cells. Dysfunction of ion channels results in a group of disorders named channelopathies,
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TLDR
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Small Molecule Investigation of KCNQ Potassium Channels: A Dissertation
TLDR
A model places calmodulin close to the gate ofKCNQ channels, providing structural insight into how CaM is able to communicate changes in intracellular calcium levels to KCNQ channel complexes.
Molecular mechanisms underlying KVS-1-MPS-1 complex assembly.
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The principles that determine the interactions of Caenorhabditis elegans MPS-1, a bifunctional beta-subunit that possesses kinase activity, with Kv channels are investigated.
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References

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Modulation of A-type potassium channels by a family of calcium sensors
TLDR
Three Kv channel-interacting proteins (KChIPs) that bind to the cytoplasmic amino termini of Kv4 α-subunits are described that may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium.
A minK–HERG complex regulates the cardiac potassium current IKr
TLDR
It is shown that HERG and minK form a stable complex, and that this heteromultimerization regulates IKr activity, which is central to the control of the heart rate and rhythm.
Coassembly of KVLQT1 and minK (IsK) proteins to form cardiac IKS potassium channel
TLDR
KVLQT1 is the subunit that coassembles with minK to form IKS channels and IKS dysfunction is a cause of cardiac arrhythmia, and is shown to encode a K+ channel with biophysical properties unlike other known cardiac currents.
MinK-Related Peptide 1 Associates With Kv4.2 and Modulates Its Gating Function: Potential Role as &bgr; Subunit of Cardiac Transient Outward Channel?
TLDR
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.
Do all voltage-gated potassium channels use MiRPs?
TLDR
It is shown that MiRP1 can alter the function of Kv4 family subunits (which contribute to I to, transient outward currents in heart and brain) when they are expressed together in Xenopus oocytes.
A constitutively open potassium channel formed by KCNQ1 and KCNE3
TLDR
It is shown that the novel β-subunit KCNE3 markedly changes KCNQ1 properties to yield currents that are nearly instantaneous and depend linearly on voltage, which indicates that these proteins may assemble to form the potassium channel that is important for cyclic AMP-stimulated intestinal chloride secretion and that is involved in secretory diarrhoea and cystic fibrosis.
A Single Transmembrane Site in the KCNE-encoded Proteins Controls the Specificity of KvLQT1 Channel Gating*
TLDR
A model of KCNE-potassium channel interaction where the functional consequence depends on the precise contact at a single amino acid is proposed, suggesting that KCNE3 traps the channel in a stable open state.
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