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(Received for publication, November 21, 1995; and in revised form, January 2, 1996)
The cAMP/cAMP-dependent protein kinase (A-kinase) and
Ca/calmodulin-dependent protein kinase (Cam-kinase)
signal transduction pathways are well known to regulate gene
transcription, but this has not been demonstrated directly for the
cGMP/cGMP-dependent protein kinase (G-kinase) signal transduction
pathway. Here we report that transfection of G-kinase into
G-kinase-deficient cells causes activation of the human c-fos promoter in a strictly cGMP-dependent manner. The effect of
G-kinase appeared to be mediated by several sequence elements, most
notably the serum response element (SRE), the AP-1 binding site (FAP),
and the cAMP response element (CRE). The magnitude of G-kinase
transactivation of the fos promoter was similar to that of
A-kinase, but there were significant differences between G-kinase and
A-kinase activation of single enhancer elements and of a chimeric
Gal4-CREB transcription factor. Our results indicate that G-kinase
transduces signals to the nucleus independently of A-kinase or
Ca
, although it may target some of the same
transcription factors as A-kinase and Cam-kinase.
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