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J Biol Chem, Vol. 275, Issue 7, 5090-5095, February 18, 2000
From the Max-Planck Institute of Immunobiology, Department of
Molecular Embryology, Stübeweg 51, D-79108 Freiburg, Germany
Casein Kinase II Phosphorylation of E-cadherin Increases
E-cadherin/
-Catenin Interaction and Strengthens Cell-Cell
Adhesion*
-Catenin, a member of the Armadillo repeat
protein family, binds directly to the cytoplasmic domain of E-cadherin,
linking it via 
-catenin to the actin cytoskeleton. A 30-amino acid
region within the cytoplasmic domain of E-cadherin, conserved among all classical cadherins, has been shown to be essential for -catenin binding. This region harbors several putative casein kinase II (CKII)
and glycogen synthase kinase-3 (GSK-3) phosphorylation sites and
is highly phosphorylated. Here we report that in vitro this
region is indeed phosphorylated by CKII and GSK-3, which results in
an increased binding of -catenin to E-cadherin. Additionally, in
mouse NIH3T3 fibroblasts expression of E-cadherin with mutations in
putative CKII sites resulted in reduced cell-cell contacts. Thus,
phosphorylation of the E-cadherin cytoplasmic domain by CKII and
GSK-3 appears to modulate the affinity between -catenin and
E-cadherin, ultimately modifying the strength of cell-cell adhesion.
*
This work was supported by the Max-Planck Society.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.: +49-761-5108475;
Fax: +49-761-5108474; E-mail: stappert@immunbio.mpg.de.
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