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

D. P. Mohapatra, K. S. Park, James Trimmer

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

Voltage-gated K+ channels are key regulators of neuronal excitability. The Kv2.1 voltage-gated K+ channel is the major delayed rectifier K+ channel expressed in most central neurons, where it exists as a highly phosphorylated protein. Kv2.1 plays a critical role in homoeostatic regulation of intrinsic neuronal excitability through its activity- and calcineurin-dependent dephosphorylation. Here, we review studies leading to the identification and functional characterization of in vivo Kv2.1 phosphorylation sites, a subset of which contribute to graded modulation of voltage-dependent gating. These findings show that distinct developmental-, cell- and state-specific regulation of phosphorylation at specific sites confers a diversity of functions on Kv2.1 that is critical to its role as a regulator of intrinsic neuronal excitability.

Original languageEnglish (US)
Pages (from-to)1064-1068
Number of pages5
JournalBiochemical Society Transactions
Volume35
Issue number5
DOIs
StatePublished - Nov 2007

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Keywords

  • Calcineurin
  • Electrical signalling
  • Ion channel
  • Mass spectrometry
  • Neuron
  • Protein kinase

ASJC Scopus subject areas

  • Biochemistry

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