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J Biol Chem, Vol. 273, Issue 24, 14950-14957, June 12, 1998
From the The
Characterization of CCAAT/Enhancer-binding Protein
as a
Cyclic AMP-responsive Nuclear Regulator
,
Department of Biochemistry, University of
Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada and the
¶ Department of Pharmacology, University of Tennessee,
Memphis, Tennessee 38163
isoform of CCAAT/enhancer-binding protein
(C/EBP) is a transcription factor that regulates expression of genes
linked to adipose differentiation and hepatic nutrient metabolism.
Recently, our laboratory has characterized a role for C/EBP in
mediating hormonal responsiveness. For example, the cAMP responsiveness of the phosphoenolpyruvate carboxykinase gene promoter in liver requires synergism among the cAMP response element-binding protein (CREB), C/EBP, and activator protein-1. In the present study, we
show that C/EBP can functionally substitute for CREB in this cAMP
response unit, i.e. cAMP responsiveness can occur in the absence of CREB. This observation is physiologically relevant since
both CREB and C/EBP have been shown to bind with high affinity to
the cAMP response element in this particular promoter.
Structure/function analysis of C/EBP identified specific mutations
that differentially affected its constitutive and protein kinase
A-inducible activities. This finding suggests that the mechanism
whereby C/EBP mediates constitutive transactivation is distinct from
that whereby it mediates cAMP responsiveness. These data support the
hypothesis that C/EBP plays a critical role in metabolism, in part
by participating in the hormonal regulation of expression of
metabolically important genes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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