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J. Biol. Chem., Vol. 266, Issue 28, 18431-18434, 10, 1991
RP Rehfuss, KM Walton, MM Loriaux and RH Goodman
Many promoters respond transcriptionally to elevated levels of cAMP through
the cAMP-responsive enhancer (CRE). Several proteins have been
characterized which bind to the CRE and presumably modulate CRE- dependent
transcription. Of these CRE-binding proteins, only CREB has been shown to
be activated by cAMP-dependent protein kinase A (PKA), and as such, CREB
represents the only basis for our understanding of cAMP-regulated
transcriptional activity. In this report, we describe the complete cDNA
sequence of another CRE-binding protein, ATF-1. This protein contains a
consensus phosphorylation site for PKA and shares extensive homology with
CREB in the region surrounding and carboxyl- terminal to the PKA site.
ATF-1 does not contain sequences homologous to the glutamine-rich
amino-terminal domain found in CREB, however. ATF- 1, like CREB, is
expressed in a wide variety of cell types, and ATF-1 is capable of
dimerizing with CREB. Both ATF-1 homodimers and ATF- 1/CREB heterodimers
bind to the CRE but not to the related phorbol ester response element.
ATF-1 is as active as CREB in its ability to mediate the transcriptional
effects of PKA, and, because ATF-1 has a smaller effect on basal
expression, it is actually more responsive than CREB to cAMP. These
findings indicate that CREB is not unique in its ability to mediate
cAMP-dependent transcriptional regulation.
The cAMP-regulated enhancer-binding protein ATF-1 activates transcription in response to cAMP-dependent protein kinase A
Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
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