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(Received for publication, April 2, 1996, and in revised form, July 19, 1996)
From the Department of Pharmacological and Physiological Sciences,
Saint Louis University School of Medicine,
St. Louis, Missouri 63104
CREB-binding protein (CBP) functions as a
coactivator molecule for a number of transcription factors including
CREB, c-Fos, c-Jun, c-Myb, and several nuclear receptors. Although
binding sites for these factors within CBP have been identified, the
regions of CBP responsible for transcriptional activation are unknown.
In this report, we show that the N-terminal half of CBP is sufficient
for activation of CREB-mediated transcription and that this region
contains a strong transcriptional activation domain (TAD). Both
deletion of this TAD or sequestering of factors that the TAD binds
using a squelching assay were found to greatly decrease the ability of
CBP to activate CREB-mediated transcription. In vivo
studies by others have shown that p300/CBP associates with TBP; using
an in vitro approach, we show the N-terminal TAD binds TBP.
We also examined the ability of the C terminus of CBP to activate
transcription using GAL-CBP chimeras. With this approach, we identified
two C-terminal TADs located adjacent to the c-Fos binding site. In
previous studies, cAMP-dependent protein kinase A (PKA)
increased the transcriptional activity of a GAL full-length CBP chimera
in F9 cells, and of the C terminus in PC-12 cells. Here, we demonstrate
that PKA also increased the ability of the N-terminal TADs of CBP to
activate transcription in PC-12 but not F9 or COS-7 cells, suggesting
that this PKA-responsiveness is cell type-specific.
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28138-28145
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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