Abstract
The small guanosine triphosphatases (GTPases) Cdc42 and Rac1 regulate E-cadherin-mediated cell-cell adhesion. IQGAP1, a target of Cdc42 and Rac1, was localized with E-cadherin and beta-catenin at sites of cell-cell contact in mouse L fibroblasts expressing E-cadherin (EL cells), and interacted with E-cadherin and beta-catenin both in vivo and in vitro. IQGAP1 induced the dissociation of alpha-catenin from a cadherin-catenin complex in vitro and in vivo. Overexpression of IQGAP1 in EL cells, but not in L cells expressing an E-cadherin-alpha-catenin chimeric protein, resulted in a decrease in E-cadherin-mediated cell-cell adhesive activity. Thus, IQGAP1, acting downstream of Cdc42 and Rac1, appears to regulate cell-cell adhesion through the cadherin-catenin pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cadherins / metabolism*
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Cell Adhesion*
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Cell Cycle Proteins / metabolism*
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Cell Membrane / metabolism
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Cytoskeletal Proteins / metabolism
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GTP Phosphohydrolases / metabolism*
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GTP-Binding Proteins / metabolism*
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GTPase-Activating Proteins
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L Cells
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Mice
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Mutation
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Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / metabolism
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Trans-Activators*
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alpha Catenin
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beta Catenin
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cdc42 GTP-Binding Protein
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rac GTP-Binding Proteins
Substances
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CTNNB1 protein, mouse
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Cadherins
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Cell Cycle Proteins
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Ctnna1 protein, mouse
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Cytoskeletal Proteins
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GTPase-Activating Proteins
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Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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Trans-Activators
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alpha Catenin
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beta Catenin
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GTP Phosphohydrolases
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GTP-Binding Proteins
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cdc42 GTP-Binding Protein
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rac GTP-Binding Proteins