E- and 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, intracellularly, they interact with the actin-based cytoskeleton. Several intracellular proteins, collectively termed catenins, have been noted to co-immunoprecipitate with E- and N-cadherin and are thought to be involved in linking the cadherins to the cytoskeleton. Two catenins have been identified recently: a 102-kD vinculin-like protein (alpha-catenin) and a 92-kD Drosophila armadillo/plakoglobin-like protein (beta-catenin). Here, we show that plakoglobin, or an 83-kD plakoglobin-like protein, co-immunoprecipitates and colocalizes with both E- and N-cadherin. The 83-kD protein is immunologically distinct from the 92-kD beta-catenin and, because of its molecular mass, likely represents the cadherin-associated protein called gamma-catenin. Thus, two different members of a plakoglobin family associate with N- and E-cadherin and, together with the 102-kD alpha-catenin, appear to participate in linking the cadherins to the actin-based cytoskeleton.
Article|
August 01 1992
Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin.
K A Knudsen,
K A Knudsen
Lankenau Medical Research Center, Wynnewood, Pennsylvania 19096.
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M J Wheelock
M J Wheelock
Lankenau Medical Research Center, Wynnewood, Pennsylvania 19096.
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K A Knudsen
Lankenau Medical Research Center, Wynnewood, Pennsylvania 19096.
M J Wheelock
Lankenau Medical Research Center, Wynnewood, Pennsylvania 19096.
Online Issn: 1540-8140
Print Issn: 0021-9525
J Cell Biol (1992) 118 (3): 671–679.
Citation
K A Knudsen, M J Wheelock; Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin.. J Cell Biol 1 August 1992; 118 (3): 671–679. doi: https://doi.org/10.1083/jcb.118.3.671
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