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J Biol Chem, Vol. 273, Issue 24, 14920-14924, June 12, 1998
-Adrenergic Modulation of Large Conductance,
Calcium-activated Potassium (Maxi-K) Channels in Xenopus
Oocytes
From the Department of Animal Biology, School of Veterinary
Medicine, University of Pennsylvania,
Philadelphia, Pennsylvania 19104-6046
The human large conductance, calcium-activated
potassium (maxi-K) channel (
and 
subunits) and
2-adrenergic receptor genes were coexpressed in
Xenopus oocytes in order to study the mechanism of
-adrenergic modulation of channel function. Isoproterenol and
forskolin increased maxi-K potassium channel currents in
voltage-clamped oocytes expressing the receptor and both channel
subunits by 33 ± 5% and 35 ± 8%, respectively, without
affecting current activation or inactivation. The percentage of
stimulation by isoproterenol and forskolin was not different in oocytes
coexpressing the and subunits versus those
expressing the only the subunit, suggesting that the subunit is
the target for regulation. The stimulatory effect of isoproterenol was
almost completely blocked by intracellular injection of the cyclic AMP
dependent protein kinase (cAMP-PK) regulatory subunit, whereas
injection of a cyclic GMP dependent protein kinase inhibitory peptide
had little effect, indicating that cellular coupling of
2-adrenergic receptors to maxi-K channels involves
endogenous cAMP-PK. Mutation of one of several potential consensus
cAMP-PK phosphorylation sites (serine 869) on the subunit almost
completely inhibited -adrenergic receptor/channel stimulatory
coupling, whereas forskolin still stimulated currents moderately
(16 ± 4%). These data demonstrate that physiological coupling
between 2 receptors and maxi-K channels occurs by the
cAMP-PK mediated phosphorylation of serine 869 on the subunit on
the channel.
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