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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Mohapatra DP,Park KS,Trimmer JSdoi
10.1042/BST0351064subject
Has Abstractpub_date
2007-11-01 00:00:00pages
1064-8issue
Pt 5eissn
0300-5127issn
1470-8752pii
BST0351064journal_volume
35pub_type
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