Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin.
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Nieset JE, Redfield AR, Jin F, Knudsen KA, Johnson KR, Wheelock MJ
Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin.
J Cell Sci. 1997 Apr;110 ( Pt 8):1013-22.
- PubMed ID
- 9152027 [ View in PubMed]
- Abstract
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin and gamma-catenin (also known as plakoglobin), have been identified. beta-catenin or plakoglobin is associated directly with the cadherin; alpha-catenin binds to beta-catenin/plakoglobin and serves to link the cadherin/catenin complex to the actin cytoskeleton. The domains on the cadherin and betacatenin/plakoglobin that are responsible for protein-protein interactions have been mapped. However, little is known about the molecular interactions between alpha-catenin and beta-catenin/plakoglobin or about the interactions between alpha-catenin and the cytoskeleton. In this study we have used the yeast two-hybrid system to map the domains on alpha-catenin that allow it to associate with beta-catenin/plakoglobin and with alpha-actinin. We also identify a region on alpha-actinin that is responsible for its interaction with alpha-catenin. The yeast two-hybrid data were confirmed with biochemical studies.