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Volume 272, Number 17, Issue of April 25, 1997 pp. 11017-11020
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification of the Domain of alpha -Catenin Involved in Its Association with beta -Catenin and Plakoglobin (gamma -Catenin)

(Received for publication, May 21, 1996, and in revised form, December 9, 1996)

Hiroya Obama and Masayuki Ozawa

From the Department of Biochemistry, Faculty of Medicine, Kagoshima University, 8-35-1 Sakuragaoka, Kagoshima 890, Japan

alpha -Catenin is a 102-kDa protein exhibiting homology to vincuin, and it forms complexes with cadherins or the tumor-suppressor gene product adenomatous polyposis coli through binding to beta -catenin or plakoglobin (gamma -catenin). The incorporation of alpha -catenin into the cadherin-catenin complexes is a prerequisite for expression of the cell-adhesive activity of cadherins. Using an in vitro assay system involving bacterially expressed proteins, we localized a region in alpha -catenin required for molecular interaction with beta -catenin and plakoglobin. Analysis of various truncated alpha -catenin molecules revealed that amino-terminal residues 48-163 are able to bind to beta -catenin and plakoglobin. Consistent with the observation that beta -catenin and plakoglobin bind to the same region of alpha -catenin, beta -catenin competed with the binding of plakoglobin to alpha -catenin and vice versa. Under the conditions used, beta -catenin bound to alpha -catenin with higher affinity than did plakoglobin. Scatchard analysis indicated that the affinity of the interaction between alpha -catenin and beta -catenin or that between alpha -catenin and plakoglobin was moderately strong (Kd = 3.8 × 10-8 and 7.7 × 10-8, respectively). When transfected into L cells expressing E-cadherin, the amino-terminal region of alpha -catenin (from residue 1 to 226) formed complexes with beta -catenin supporting the in vitro binding experiment results.


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