Plakoglobin, or an 83-kD Homologue Distinct from / -catenin, Interacts with E-cadherin and N-cadherin

Abstract

Eand N-cadherin are members of a family of calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. Extracellularly, the transmembrane cadherins self-associate, while, intracellulady, they interact with the actin-based cytoskeleton. Several intracellular proteins, collectively termed catenins, have been noted to co-immunoprecipitate with Eand N-cadherin and are thought to be involved in linking the cadherins to the cytoskeleton. Two catenins have been identified recently: a 102-kD vinculinlike protein (ot-catenin) and a 92-kD Drosophila armadillo/plakoglobin-like protein (13-catenin). Here, we show that plakoglobin, or an 83-kD plakoglobin-like protein, co-immunoprecipitates and colocalizes with both Eand N-cadherin. The 83-kD protein is immunologicaUy distinct from the 92-kD ~-catenin and, because of its molecular mass, likely represents the cadherin-associated protein called ~/-catenin. Thus, two different members of a plakoglobin family associate with Nand E-cadherin and, together with the 102-kD ot-catenin, appear to participate in linking the cadherins to the actin-based

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@inproceedings{Knudsen2002PlakoglobinOA, title={Plakoglobin, or an 83-kD Homologue Distinct from / -catenin, Interacts with E-cadherin and N-cadherin}, author={Karen A. Knudsen}, year={2002} }