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J Biol Chem, Vol. 274, Issue 25, 18017-18025, June 18, 1999
From Max-Planck-Institute of Immunobiology, Stuebeweg 51, D-79108 Freiburg, Germany
Functional Characterization of Multiple Transactivating Elements
in
-Catenin, Some of Which Interact with the TATA-binding Protein
in Vitro
-Catenin, a member of the family of Armadillo
repeat proteins, plays a dual role in cadherin-mediated cell adhesion
and in signaling by Wnt growth factors. Upon Wnt stimulation
-catenin undergoes nuclear translocation and serves as
transcriptional coactivator of T cell factor DNA-binding proteins.
Previously the transactivation potential of different portions of
-catenin has been demonstrated, but the precise location of
transactivating elements has not been established. Also, the mechanism
of transactivation by -catenin and the molecular basis for
functional differences between -catenin and the closely related
proteins Armadillo and Plakoglobin are poorly understood. Here we have
used a yeast system for the detailed characterization of the
transactivation properties of -catenin. We show that its
transactivation domains possess a modular structure, consist of
multiple subelements that cover broad regions at its N and C termini,
and extend considerably into the Armadillo repeat region. Compared with
-catenin the N termini of Plakoglobin and Armadillo have different
transactivation capacities that may explain their distinct signaling
properties. Furthermore, transactivating elements of -catenin
interact specifically and directly with the TATA-binding protein
in vitro providing further evidence that a major function
of -catenin during Wnt signaling is to recruit the basal
transcription machinery to promoter regions of Wnt target genes.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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