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J Biol Chem, Vol. 275, Issue 1, 585-598, January 7, 2000
From the Department of Cell Biology and Physiology, University of
Pittsburgh, Pittsburgh, Pennsylvania 15261
We determined the effect of nucleotides and
protein kinase A (PKA) on the
Ca2+-dependent gating of the cloned
intermediate conductance, Ca2+-dependent
K+ channel, hIK1. In Xenopus oocytes, during
two-electrode voltage-clamp, forskolin plus isobutylmethylxanthine
induced a Ca2+-dependent increase in hIK1
activity. In excised inside-out patches, addition of ATP induced a
Ca2+-dependent increase in hIK1 activity
(NPo). In contrast, neither nonhydrolyzable (AMP-PNP,
AMP-PCP) nor hydrolyzable ATP analogs (GTP, CTP, UTP, and ITP)
activated hIK1. The ATP-dependent activation of hIK1
required Mg2+ and was reversed by either exogenous alkaline
phosphatase or the PKA inhibitor PKI5-24. The
Ca2+ dependence of hIK1 activation was best fit with a
stimulatory constant (Ks) of 350 nM and
a Hill coefficient (n) of 2.3. ATP increased
NPo at [Ca2+] >100 nM while
having no effect on Ks or n. Mutation of the single PKA consensus phosphorylation site at serine 334 to
alanine (S334A) had no effect on the PKA-dependent
activation during either two-electrode voltage-clamp or in excised
inside-out patches. When expressed in HEK293 cells, ATP activated hIK1
in a Mg2+-dependent fashion, being reversed by
alkaline phosphatase. Neither PKI5-24 nor
CaMKII281-309 or PKC19-31 affected the
ATP-dependent activation. Northern blot analysis revealed hIK1 expression in the T84 colonic cell line. Endogenous hIK1 was
activated by ATP in a Mg2+- and
PKI5-24-dependent fashion and was reversed by
alkaline phosphatase, whereas CaMKII281-309 and
PKC19-31 had no effect on the ATP-dependent
activation. The Ca2+-dependent activation
(Ks and n) was unaffected by ATP. In
conclusion, hIK1 is activated by a membrane delimited PKA when endogenously expressed. Although the oocyte expression system recapitulates this regulation, expression in HEK293 cells does not. The
effect of PKA on hIK1 gating is Ca2+-dependent
and occurs via an increase in NPo without an effect on
either Ca2+ affinity or apparent cooperativity.
Kinase-dependent Regulation of the Intermediate
Conductance, Calcium-dependent Potassium Channel,
hIK1*
*
This work was supported by Cystic Fibrosis Foundation Grant
DEVOR 96P0, Competitive Medical Research Fund University of Pittsburgh Medical Center Grant 3976-1000, and National Institutes of Health Grant
DK54941-01 (to D. C. D.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell Biology
and Physiology, S312 Biomedical Science Tower, University of
Pittsburgh, 3500 Terrace St., Pittsburgh, PA 15261. E-mail: dd2+@pitt.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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