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Abstract
The DF3/MUC1 mucin-like glycoprotein is aberrantly overexpressed in human breast carcinomas. The functional role of DF3 is unknown. The present studies demonstrate that DF3 associates with beta-catenin. Similar findings have been obtained for gamma-catenin but not alpha-catenin. DF3, like E-cadherin and the adenomatous polyposis coli gene product, contains an SXXXXXSSL site that is responsible for direct binding to beta-catenin. The results further demonstrate that interaction of DF3 and beta-catenin is dependent on cell adhesion. These findings and the role of beta-catenin in cell signaling support a role for DF3 in the adhesion of epithelial cells.
Highlights
The human DF3 (MUC1, episialin, PEM) gene encodes a high molecular mass membrane-associated glycoprotein with a mucin-like external domain
Cadherin cell adhesion molecules form complexes with the cytoplasmic ␣, , and ␥-catenin proteins (13). ␣-Catenin is required for cadherin-mediated cell adhesion and links cadherins to the actin cytoskeleton (14, 15). -Catenin links ␣-catenin to the cadherins and is highly related to plakoglobin (␥catenin) (16 –18). -Catenin is homologous to the Drosophila segment polarity gene product Armadillo (19) that acts downstream of Wingless (20)
Other studies have demonstrated that -catenin binds directly to the adenomatous polyposis coli (APC)1 gene product (23–25)
Summary
The human DF3 (MUC1, episialin, PEM) gene encodes a high molecular mass membrane-associated glycoprotein with a mucin-like external domain. Cadherin cell adhesion molecules form complexes with the cytoplasmic ␣-, -, and ␥-catenin proteins (13). Other studies have demonstrated that -catenin binds directly to the adenomatous polyposis coli (APC)1 gene product (23–25). We demonstrate that cell adhesion induces the interaction between DF3 and -catenin.
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