JBC Transcription and Nuclear Factor Monoclonals

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Volume 271, Number 9, Issue of March 1, 1996 pp. 4597-4600
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Regulation of Gene Expression by cGMP-dependent Protein Kinase
TRANSACTIVATION OF THE c-fos PROMOTER

(Received for publication, November 21, 1995; and in revised form, January 2, 1996)

Tanima Gudi Ivana Huvar Matthias Meinecke Suzanne M. Lohmann Gerry R. Boss Renate B. Pilz

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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