Abstract
Cadherin-mediated cell-cell interactions are modulated by protein interactions at the cytoplasmic face of the membrane. Recent work has shown that phosphorylation of both p120(ctn) and beta-catenin affects their interaction with cadherins and the molecular connections to the cytoskeleton. The cytoskeletal connections most probably include interactions between alpha-catenin, and/or alpha-actinin, vinculin, ZO-1, actin and possibly spectrin.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Armadillo Domain Proteins
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Cadherins / chemistry
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Cadherins / physiology*
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Calcium / metabolism
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Catenins
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Cell Adhesion / physiology*
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Cell Adhesion Molecules / metabolism
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Cytoplasm / ultrastructure*
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Cytoskeletal Proteins / metabolism
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Delta Catenin
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Dimerization
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Drosophila Proteins*
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Humans
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Insect Proteins / chemistry
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Macromolecular Substances
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Multigene Family
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Phosphoproteins / metabolism
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Phosphorylation
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Protein Binding
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Spectrin / metabolism
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Trans-Activators*
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Vinculin / metabolism
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alpha Catenin
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beta Catenin
Substances
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Armadillo Domain Proteins
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CTNNA1 protein, human
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CTNNB1 protein, human
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Cadherins
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Catenins
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Cell Adhesion Molecules
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Cytoskeletal Proteins
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Drosophila Proteins
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Insect Proteins
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Macromolecular Substances
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Phosphoproteins
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Trans-Activators
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alpha Catenin
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beta Catenin
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Vinculin
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Spectrin
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Calcium
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Delta Catenin
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CTNND1 protein, human