Modification of delayed rectifier potassium currents by the Kv9.1 potassium channel subunit

@article{Richardson2000ModificationOD,
 title={Modification of delayed rectifier potassium currents by the Kv9.1 potassium channel subunit},
 author={Frank C. Richardson and Leonard K. Kaczmarek},
 journal={Hearing Research},
 year={2000},
 volume={147},
 pages={21-30},
 url={https://api.semanticscholar.org/CorpusID:21065404}
}

54 Citations

Protein Kinase C Modulates Inactivation of Kv3.3 Channels*
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Regulation of Kv2.1 Channels by Kv9.1 Variants
The Ile489Val substitution in Kv9.1 does not disrupt its ability to co-assemble with Kv2 channels, nor its effects on the voltage-dependence of channel gating, but it did produce a greater reduction in the Kv2.1 surface expression, suggesting that this underlies its association with pain hypersensitivity.

Slack and Slick KNa Channels Regulate the Accuracy of Timing of Auditory Neurons
Manipulations of the level of KNa current in MNTB neurons, either by increasing levels of internal Na+ or by exposure to a pharmacological activator of Slack channels, significantly enhance the accuracy of timing of action potentials at high frequencies of stimulation.

Kv2.1 and silent Kv subunits underlie the delayed rectifier K+ current in cultured small mouse DRG neurons.
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...

22 References

Depolarization Selectively Increases the Expression of the Kv3.1 Potassium Channel in Developing Inferior Colliculus Neurons
Depolarization and calcium influx may alter the excitability of immature inferior colliculus neurons by selectively increasing the levels of a Kv3.1-like potassium current, when expressed heterologously.

Kv8.1, a new neuronal potassium channel subunit with specific inhibitory properties towards Shab and Shaw channels.
Outward rectifier K+ channels have a characteristic structure with six transmembrane segments and one pore region, and a new member of this family of trans Membrane proteins has been cloned and called Kv8.1, which abolishes the functional expression of members of the Kv2 and Kv3 subfamilies, suggesting that the functional role of this member might be to inhibit the function of a particular class of outward rectifiers.

New Modulatory α Subunits for Mammalian ShabK+ Channels*
The changes in electrophysiological properties of Kv2 subunits induced by Kv5.1 and Kv6.1, two other modulatory subunits are analyzed to provide an amazingly new capacity of functional diversity.

Contribution of the Kv3.1 potassium channel to high‐frequency firing in mouse auditory neurones
Analysis of patch‐clamp, in situ hybridization and computer simulation techniques concludes that in mouse MNTB neurones the Kv3.1 channel contributes to the ability of these cells to lock their firing to high‐frequency inputs.

Localization of a high threshold potassium channel in the rat cochlear nucleus
The pattern of immunolabeling revealed that the Kv3.1 protein is distributed along the soma, proximal dendrites, unmyelinated axons, and axon terminals of stained neurons, which enhances the ability of a model cell with some of the features of bushy cells to follow high frequency input with temporal precision.

Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes
Evidence that the Shaker A-type K+ channels expressed in Xenopus oocytes contain several Shaker polypeptides is provided, and it is suggested that heteromultimer formation may increase K+ channel diversity beyond even the level expected from the large number of K+Channel genes and alternative splicing products.

Kv2.1/Kv9.3, a novel ATP‐dependent delayed‐rectifier K+ channel in oxygen‐sensitive pulmonary artery myocytes
It is proposed that metabolic regulation of the Kv2.1/Kv9.3 heteromultimer may play an important role in hypoxic PA vasoconstriction and in the possible development of PA hypertension.

Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits
These findings indicate that some intermediate-conductance channels in the nervous system may result from an interaction between Slack and Slo channel subunits, and are activated by cytoplasmic calcium.

Subunit Assembly and Domain Analysis of Electrically Silent K+ Channel α‐Subunits of the Rat Kv9 Subfamily
Abstract:α‐Subunits of the voltage‐gated potassium channel (Kv) subfamily Kv9 show no channel activity after homomultimeric expression in heterologous expression systems. This report shows that...

Modes of Regulation of Shab K+ Channel Activity by the Kv8.1 Subunit*
The Kv8.1 subunit expressed at high levels acts as a specific suppressor of the activity of Kv2 and Kv3 channels in Xenopus oocytes and forms hybrid Kv 8.1/Kv2 channels, which have new biophysical properties and more particularly modified properties of the inactivation process as compared with homopolymers of K v2.1 or KV2.2 channels.