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J. Biol. Chem., Vol. 276, Issue 23, 20436-20443, June 8, 2001
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From the ¶ Unitat de Biologia Cel.lular i Molecular, Institut
Municipal d'Investigació Mèdica, Universitat Pompeu Fabra,
c/Dr. Aiguader 80, 08003 Barcelona, Spain and
Regulation of
-Catenin Structure and Activity by
Tyrosine Phosphorylation*
§,,,§,
, and
Unitat de
Biofísica, Departament de Bioquímica i Biologia
Molecular, Facultat de Medicina, Universitat Autònoma de
Barcelona, 08193 Bellaterra, Spain
-Catenin plays a dual role as a key effector
in the regulation of adherens junctions and as a transcriptional
coactivator. Phosphorylation of Tyr-654, a residue placed in the last
armadillo repeat of -catenin, decreases its binding to E-cadherin.
We show here that phosphorylation of Tyr-654 also stimulates the
association of -catenin to the basal transcription factor
TATA-binding protein. The structural bases of these different
affinities were investigated. Our results indicate that the -catenin
C-terminal tail interacts with the armadillo repeat domain, hindering
the association of the armadillo region to the TATA-binding protein or
to E-cadherin. Phosphorylation of -catenin Tyr-654 decreases
armadillo-C-terminal tail association, uncovering the last armadillo
repeats. In a C-terminal-depleted -catenin, the presence of a
negative charge at Tyr-654 does not affect the interaction of the
TATA-binding protein to the armadillo domain. However, in the case of
E-cadherin, the establishment of ion pairs dominates its association
with -catenin, and its binding is greatly dependent on the absence of a negative charge at Tyr-654. Thus, phosphorylation of Tyr-654 blocks the Ecadherin--catenin interaction, even though the
steric hindrance of the C-tail is no longer present. These results
explain how phosphorylation of -catenin in Tyr-654 modifies the
tertiary structure of this protein and the interaction with its
different partners.
*
This work was supported by La Marató de TV3 Grant
983110 (to A. G. H.), Ministerio de Ciencia y Tecnología
Grant PM99-0064 (to M. D.), FEDER-Fondo Nacional I+D Fund Grants
2FD97-1491-C02-01 and 2FD97-1491-C02-02 (to A. G. H. and
M. D., respectively), and Direcció General de Recerca Grants
1999SGR00245 and 1999SGR00102.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
34-93-581-1870; Fax: 34-93-581-1907; E-mail: mireia.dunach@uab.es (for
M. Duñach) or Tel.: 34-93-221-1009; Fax: 34-93-221-3237; E-mail: agarcia@imim.es (for A. Garcia de Herreros)
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