© The Rockefeller University Press,
0021-9525/1999//1311 $5.00
The Journal of Cell Biology, Volume 144, Number 6,
, 1999 1311-1322
Functional Domains of
-Catenin Required for the Strong State of Cadherin-based Cell Adhesion
Yuzo Imamura,
Masahiko Itoh,
Yoshito Maeno,
Shoichiro Tsukita, and
Akira Nagafuchi
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.
Key Words:
-catenin ZO-1 vinculin E-cadherin adhesion
Abbreviations used in this paper: AJ, adherens junctions; TJ, tight junction.

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