What does this research mean for the field?

Multisite phosphorylation of the Kv2.1 potassium channel dynamically regulates its voltage-dependent gating, conferring diverse functions critical for controlling intrinsic neuronal excitability. Novelty: ClaimNovelty.SYNTHESIS. Consensus alignment: ConsensusAlignment.NEUTRAL.

October 25, 2007Biochemical Society Transactions

Dynamic regulation of the voltage-gated Kv2.1 potassium channel by multisite phosphorylation

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Population

Basic science review focusing on the Kv2.1 voltage-gated K(+) channel in central neurons

Design

Review

Authors

DMDurga P. MohapatraNational Institutes of Health KPK.-S. ParkUniversity of California, Davis JTJames S. TrimmerElectrophysiology

Discussion

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Implication

Kv2.1 phosphorylation diversity informs neuronal excitability; leaves open targeted therapies pending further study.

Structured PICO

Population

Basic science review focusing on the Kv2.1 voltage-gated K(+) channel in central neurons

This review highlights the critical role of multisite phosphorylation in regulating the Kv2.1 potassium channel and intrinsic neuronal excitability.

Cite This Study

Mohapatra et al. (2007) studied this question.

synapsesocial.com/papers/6a19dafa4b45427442ead104 https://doi.org/10.1042/bst0351064

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Dynamic regulation of the voltage-gated Kv2.1 potassium channel by multisite phosphorylation

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Dynamic regulation of the voltage-gated Kv2.1 potassium channel by multisite phosphorylation

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider