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J Biol Chem, Vol. 273, Issue 24, 14920-14924, June 12, 1998

Reconstitution of -Adrenergic Modulation of Large Conductance, Calcium-activated Potassium (Maxi-K) Channels in Xenopus Oocytes
IDENTIFICATION OF THE cAMP-DEPENDENT PROTEIN KINASE PHOSPHORYLATION SITE

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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