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J. Cell Biol.,
Volume 144, Number 6, March 22, 1999 1311-1322
-Catenin Required for the Strong State of
Cadherin-based Cell Adhesion
Department of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan
The interaction of cadherin-catenin complex
with the actin-based cytoskeleton through
-catenin is
indispensable for cadherin-based cell adhesion activity.
We reported previously that E-cadherin-
-catenin fusion molecules showed cell adhesion and cytoskeleton
binding activities when expressed in nonepithelial
L cells. Here, we constructed deletion mutants of
E-cadherin-
-catenin fusion molecules lacking various
domains of
-catenin and introduced them into L cells. Detailed analysis identified three distinct functional domains of
-catenin: a vinculin/
-actinin-binding domain, a ZO-1-binding domain, and an adhesion-modulation domain. Furthermore, cell dissociation assay
revealed that the fusion molecules containing the
ZO-1-binding domain in addition to the adhesion-modulation domain conferred the strong state of cell adhesion activity on transfectants, although those lacking
the ZO-1-binding domain conferred only the weak state. The disorganization of actin-based cytoskeleton
by cytochalasin D treatment shifted the cadherin-based
cell adhesion from the strong to the weak state. In the
epithelial cells, where
-catenin was not precisely colocalized with ZO-1, the ZO-1-binding domain did not
completely support the strong state of cell adhesion
activity. Our studies showed that the interaction of
-catenin with the actin-based cytoskeleton through
the ZO-1-binding domain is required for the strong
state of E-cadherin-based cell adhesion activity.
-catenin;
ZO-1;
vinculin;
E-cadherin;
adhesion
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