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J Biol Chem, Vol. 273, Issue 45, 29524-29529, November 6, 1998
-Catenin That Plays an
Essential Role in Cadherin-mediated Cell Adhesion
From the Department of Biochemistry, Faculty of Medicine, Kagoshima
University, Kagoshima 890-8520, Japan
-Catenin is an intrinsic component of the
cadherin adhesion complex and is a 102-kDa protein with multiple
interaction sites, including homodimerization sites, and binding sites
for 
- and 
-catenin (plakoglobin), -actinin, and actin. Besides
the binding to - or -catenin, it is unknown, however, which
interaction is critical for the function of cadherins. By expressing a
series of E-cadherin--catenin chimeric molecules on leukemia cells
(K562), we have identified the region of -catenin that confers
aggregation inducing activity to nonfunctional tail-less E-cadherin.
The region has been mapped to the carboxyl-terminal 295 amino acids of
-catenin. Consistent with this result, expression in
-catenin-deficient cells (DLD-1/
) of a mutant -catenin
molecule consisting of the amino-terminal -/-catenin-binding site
and the carboxyl-terminal cell adhesion region identified in the above
experiments induced E-cadherin-mediated cell aggregation and
compaction. Cells expressing E-cadherin chimeric molecules with the
homologous carboxyl-terminal region of vinculin, which contains the
actin-binding site of vinculin, did not, however, aggregate as strongly
as ones expressing E-cadherin--catenin chimeric molecules.
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