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J Biol Chem, Vol. 274, Issue 16, 10927-10935, April 16, 1999
From the Department of Physiology and Cell Biology, University of
Nevada School of Medicine, Reno, Nevada 89557
NO-induced activation of
cGMP-dependent protein kinase (PKG) increases the open
probability of large conductance Ca2+-activated
K+ channels and results in smooth muscle relaxation.
However, the molecular mechanism of channel regulation by the NO-PKG
pathway has not been determined on cloned channels. The present study was designed to clarify PKG-mediated modulation of channels at the
molecular level. The cDNA encoding the
Cyclic GMP-dependent Protein Kinase Activates Cloned
BKCa Channels Expressed in Mammalian Cells by Direct
Phosphorylation at Serine 1072
-subunit of the large conductance Ca2+-activated K+ channel,
cslo-, was expressed in HEK293 cells. Whole cell and single channel characteristics of cslo- exhibited
functional features of native large conductance
Ca2+-activated K+ channels in smooth muscle
cells. The NO-donor sodium nitroprusside increased outward current
2.3-fold in whole cell recordings. In cell-attached patches, sodium
nitroprusside increased the channel open probability (NPo) of
cslo- channels 3.3-fold without affecting unitary
conductance. The stimulatory effect of sodium nitroprusside was
inhibited by the PKG-inhibitor KT5823. Direct application of PKG-I
to the cytosolic surface of inside-out patches increased NPo 3.2-fold
only in the presence of ATP and cGMP without affecting unitary
conductance. A point mutation of cslo- in which Ser-1072 (the only optimal consensus sequence for PKG phosphorylation) was
replaced by Ala abolished the PKG effect on NPo in inside-out patches
and the effect of SNP in cell attached patches. These results indicate
that PKG activates cslo- by direct phosphorylation at
serine 1072.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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