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J Biol Chem, Vol. 274, Issue 13, 8391-8404, March 26, 1999
From the Department of Biological Chemistry and the Mental Health
Research Institute, University of Michigan,
Ann Arbor, Michigan 48109
The ability of cGMP-dependent protein
kinases (cGKs) to activate cAMP response element
(CRE)-dependent gene transcription was compared with that
of cAMP-dependent protein kinases (cAKs). Although both the
type I
Cyclic AMP- and Cyclic GMP-dependent Protein Kinases
Differ in Their Regulation of Cyclic AMP Response
Element-dependent Gene Transcription
cGMP-dependent protein kinase (cGKI) and the
type II cAMP-dependent protein kinase (cAKII)
phosphorylated the cytoplasmic substrate VASP (vasodilator-
and A kinase-stimulated phosphoprotein) to a similar extent, cyclic nucleotide
regulation of CRE-dependent transcription was at least
10-fold higher in cAKII-transfected cells than in cGKI-transfected
cells. Overexpression of each kinase in mammalian cells resulted in a
cytoplasmic localization of the unactivated enzyme. As reported
previously, the catalytic (C) subunit of cAKII translocated to the
nucleus following activation by 8-bromo-cyclic AMP. However, cGKI
did not translocate to the nucleus upon activation by 8-bromo-cyclic
GMP. Replacement of an autophosphorylated serine
(Ser79) of cGKI with an aspartic acid resulted in
a mutant kinase with constitutive kinase activity in vitro
and in vivo. The cGKIS79D mutant localized to the
cytoplasm and was only a weak activator of CRE-dependent
gene transcription. However, an amino-terminal deletion mutant of
cGKI was found in the nucleus as well as the cytoplasm and was a
strong activator of CRE-dependent gene transcription. These
data suggest that the inability of cGKs to translocate to the nucleus
is responsible for the differential ability of cAKs and cGKs to
activate CRE-dependent gene transcription and that nuclear
redistribution of cGKs is not required for NO/cGMP regulation of gene transcription.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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