Abstract
Classical cadherins are complexed via their cytoplasmic domains with alpha-, beta- and gamma-catenin. This complex formation links cadherins to the actin filament network and to other transmembrane and cytoplasmic proteins. alpha-Catenin is homologous to vinculin, and beta-catenin to the product of the Drosophila gene armadillo, while gamma-catenin seems to be identical to plakoglobin. Catenins are part of a higher order protein structure that is of crucial importance for the adhesive function of cadherins. A working model of the construction and regulation of this multiprotein interaction is proposed.
MeSH terms
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Actins / metabolism
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Animals
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Cadherins / chemistry
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Cadherins / physiology*
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Cell Adhesion / physiology*
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / physiology*
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Cytoplasm / metabolism
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Cytoskeletal Proteins / chemistry
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Cytoskeletal Proteins / physiology*
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Desmoplakins
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Drosophila melanogaster / genetics
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Humans
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Mice
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Models, Biological
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Trans-Activators*
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alpha Catenin
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beta Catenin
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gamma Catenin
Substances
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Actins
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CTNNA1 protein, human
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CTNNB1 protein, human
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CTNNB1 protein, mouse
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Cadherins
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Cell Adhesion Molecules
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Ctnna1 protein, mouse
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Cytoskeletal Proteins
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Desmoplakins
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JUP protein, human
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Jup protein, mouse
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Trans-Activators
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alpha Catenin
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beta Catenin
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gamma Catenin