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Vol. 15, No. 24, pp. 3342-3354, December 15, 2001
-catenin transcription activation and inhibition in vitro
Regulatory Biology Laboratory, The Salk Institute for Biological
Studies, La Jolla, California 92037, USA
Transcriptional activation of Wnt/Wg-responsive genes requires the
stabilization and nuclear accumulation of 
-catenin, a dedicated
coactivator of LEF/TCF enhancer-binding proteins. Here we report that
recombinant -catenin strongly enhances binding and transactivation
by LEF-1 on chromatin templates in vitro. Interestingly, different
LEF-1 isoforms vary in their ability to bind nucleosomal templates in
the absence of -catenin, owing to N-terminal residues that repress
binding to chromatin, but not nonchromatin, templates. Transcriptional
activation in vitro requires both the armadillo (ARM) repeats and the C
terminus of -catenin, whereas the phosphorylated N terminus is
inhibitory to transcription. A fragment spanning the C terminus (CT)
and ARM repeats 11 and 12 (CT-ARM), but not the CT alone, functions as
a dominant negative inhibitor of LEF-1--cat activity in vitro and
can block ATP-dependent binding of the complex to chromatin. LEF-1--cat transactivation in vitro was also repressed by inhibitor of -catenin and Tcf-4 (ICAT), a physiological inhibitor of Wnt/Wg signaling that interacts with ARM repeats 11 and 12, and by the nonsteroidal anti-inflammatory compound, sulindac. None of these transcription inhibitors (CT-ARM, ICAT, or sulindac) could disrupt the
LEF-1--cat complex after it was stably bound to chromatin. We
conclude that the CT-ARM region of -catenin functions as a chromatin-specific activation domain, and that several inhibitors of
the Wnt/Wg pathway directly modulate LEF-1--cat activity on chromatin.
[Key Words:
Wnt signaling; -catenin; LEF-1; chromatin; transcription regulation]
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