Jr. Miller et Dr. Mcclay, CHANGES IN THE PATTERN OF ADHERENS JUNCTION-ASSOCIATED BETA-CATENIN ACCOMPANY MORPHOGENESIS IN THE SEA-URCHIN EMBRYO, Developmental biology, 192(2), 1997, pp. 310-322
beta-Catenin was originally identified biochemically as a protein that
binds E-cadherin in cultured cells and that interaction was later sho
wn to be essential for cadherin function. Independently, armadillo, th
e 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 i
nvestigations 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 membran
e, 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 subcellu
lar distribution in cells undergoing morphogenetic movements. Indicati
ve of a role in the establishment and maintenance of cell adhesion, be
ta-catenin is associated with lateral cell-cell contacts and accumulat
es at adherens junctions from cleavage stages onward. At gastrulation,
changes in junctional beta-catenin localization accompany several mor
phogenetic events. The epithelial-mesenchymal conversion that characte
rizes the ingression of both primary and secondary mesenchyme cells co
incides with a rapid and dramatic loss of adherens junction-associated
beta-catenin. In addition, epithelial cells in the archenteron displa
y 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 an
d adherens junction function during gastrulation in the sea urchin emb
ryo. (C) 1997 Academic Press.