Changes in the pattern of adherens junction-associated beta-catenin accompany morphogenesis in the sea urchin embryo

J R Miller, D R McClay
Developmental Biology 1997 December 15, 192 (2): 310-22
beta-Catenin was originally identified biochemically as a protein that binds E-cadherin in cultured cells and that interaction was later shown to be essential for cadherin function. Independently, armadillo, the beta-catenin homolog in Drosophila melanogaster, was identified as a segment polarity gene necessary for the transduction of wingless (Wnt) signals during embryonic and larval development. Recently, several investigations have also shown that beta-catenin plays a critical role in axial patterning of early Xenopus, zebrafish, and mouse embryos. In these systems, the localization of beta-catenin to the plasma membrane, cytosol, and nucleus is predictive of its role in cell adhesion and signaling. In order to examine the potential role of beta-catenin in regulating cell adhesion during embryogenesis, we cloned beta-catenin in the sea urchin Lytechinus variegatus and characterized its subcellular distribution in cells undergoing morphogenetic movements. Indicative of a role in the establishment and maintenance of cell adhesion, beta-catenin is associated with lateral cell-cell contacts and accumulates at adherens junctions from cleavage stages onward. At gastrulation, changes in junctional beta-catenin localization accompany several morphogenetic events. The epithelial-mesenchymal conversion that characterizes the ingression of both primary and secondary mesenchyme cells coincides with a rapid and dramatic loss of adherens junction-associated beta-catenin. In addition, epithelial cells in the archenteron display a significant decrease in adherens junction-associated beta-catenin levels as they undergo convergent-extension movements. These data are consistent with a role for beta-catenin in regulating cell adhesion and adherens junction function during gastrulation in the sea urchin embryo.

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