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Molecular Pharmacology, Volume 52, Issue 5, 821-828
Department of Biochemistry and Cell Biology and Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5215
The voltage-gated delayed-rectifier-type K+ channel Kv2.1
is expressed in high-density clusters on the soma and proximal
dendrites of mammalian central neurons; thus, dynamic regulation of
Kv2.1 would be predicted to have an impact on dendritic excitability. Rat brain Kv2.1 polypeptides are phosphorylated extensively, leading to
a dramatically increased molecular mass on sodium dodecyl sulfate gels.
Phosphoamino acid analysis of Kv2.1 expressed in transfected cells and
labeled in vivo with 32P shows that
phosphorylation was restricted to serine residues and that a truncation
mutant, 
C318, which lacks the last 318 amino acids in the
cytoplasmic carboxyl terminus, was phosphorylated to a much lesser
degree than was wild-type Kv2.1. Whole-cell patch-clamp studies showed
that the voltage-dependence of activation of C318 was shifted to
more negative membrane potentials than Kv2.1 without differences in
macroscopic kinetics; however, the differences in the
voltage-dependence of activation between Kv2.1 and C318 were
eliminated by in vivo intracellular application of
alkaline phosphatase, suggesting that these differences were due to
differential phosphorylation. Similar analyses of other truncation and
point mutants indicated that the phosphorylation sites responsible for the observed differences in voltage-dependent activation lie between amino acids 667 and 853 near the distal end of the Kv2.1 carboxyl terminus. Together, these parallel biochemical and electrophysiological results provide direct evidence that the voltage-dependent activation of the delayed-rectifier K+ channel Kv2.1 can be modulated
by direct phosphorylation of the channel protein; such modulation of
Kv2.1 could dynamically regulate dendritic excitability.
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