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Vol. 12, No. 15, pp. 2269-2277, August 1, 1998
1 Howard Hughes Medical Institute,
2 Gene
Expression Laboratory and
3 Molecular Neurobiology Laboratory,
The Salk Institute for Biological Studies, La Jolla, California 92037 USA;
4 Department of Genetics, University of Pennsylvania,
School of Medicine, Philadelphia, Pennsylvania 19104 USA
The Delta-Notch signal transduction pathway has widespread roles
in animal development in which it appears to control cell fate.
CBF1/RBP-J
, the mammalian homolog of
Drosophila Suppressor of Hairless [Su(H)], switches from a
transcriptional repressor to an activator upon Notch activation. The
mechanism whereby Notch regulates this switch is not clear. In this
report we show that prior to induction CBF1/RBP-J
interacts with a corepressor complex containing SMRT
(silencing mediator of
retinoid and thyroid hormone receptors) and
the histone deacetylase HDAC-1. This complex binds via the CBF1
repression domain, and mutants defective in repression fail to interact
with the complex. Activation by Notch disrupts the formation of the
repressor complex, thus establishing a molecular basis for the Notch
switch. Finally, ESR-1, a Xenopus gene activated by
Notch and X-Su(H), is induced in animal caps treated with TSA, an
inhibitor of HDAC-1. The functional role for the
SMRT/HDAC-1 complex in CBF1/RBP-J
regulation reveals a novel genetic switch in which extracellular
ligands control the status of critical nuclear cofactor complexes.
[Key Words:
Notch; transcriptional repressor; corepressor complex; SMRT; CBF1/RBP-J]
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