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Distinct cadherin—catenin complexes in Ca 2+ dependent cell—cell adhesion
Author(s) -
Butz Stefan,
Kemler Rolf
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01205-9
Subject(s) - plakoglobin , cadherin , catenin , cell adhesion molecule , microbiology and biotechnology , cell adhesion , biology , chemistry , cell , genetics , wnt signaling pathway , signal transduction
Catenins are peripheral cytoplasmic proteins originally identified in association with the mouse epithelial cell adhesion molecule E‐cadherin. Molecular cloning and primary structure analysis demonstrated that α‐catenin is homologous to vinculin and that β‐catenin is homologous to human plakoglobin and the Drosophila gene product armadillo . With the use of peptide‐specific anti plakoglobin antibodies we confirm here that plakoglobin is a component of the cadherin‐catenin complex and that it is most likely identical to γ‐catenin. We show that plakoglobin binds directly to E‐cadherin. We consolidate the biochemical evidence for the existence of two distinct and separable E‐cadherin‐catenin complexes in the same cell. One complex is composed of E‐cadherin, α‐and β‐catenin, the other of E‐cadherin, α‐catenin and plakoglobin. A similar distinct association with catenins is also found for other cadherins. Comparison of different cell lines revealed that the relative amounts of the two complexes vary depending on cell types.