T. Kurth et al., Immunocytochemical studies of the interactions of cadherins and catenins in the early Xenopus embryo, DEV DYNAM, 215(2), 1999, pp. 155-169
Linkage of cadherins to the cytoskeleton is crucial for their adhesive func
tion. Since alpha- and beta-catenin play a key role in this linkage, these
proteins are possible targets for processes that control cell-cell adhesion
. To achieve a better understanding of the regulation of cell-cell adhesion
in embryonic morphogenesis, we used immunohistology to investigate how in
Xenopus blastomeres catenins respond to disturbances in the expression of m
aternal cadherins, Overexpression of myc-tagged maternal cadherin leads to
a proportionate increase of the level of beta-catenin. The two proteins col
ocalize in the endoplasmic reticulum, in cytoplasmic vesicles, and along th
e cell membrane, indicating that the beta-catenin binds to overexpressed ca
dherin early in its passage to the plasma membrane. Expression of cadherin
is essential for the stable presence of beta-catenin, as depletion from mat
ernal cadherin mRNA leads to a complete loss of beta-catenin from the blast
omeres. alpha-catenin behaves differently Overexpression of cadherin leaves
the amount and localization of alpha-catenin largely unaffected, and addit
ional cadherin inserts itself into the membrane without a proportionate ris
e in the level of membrane-bound alpha-catenin, However, cadherin mRNA depl
etion leads to a redistribution of alpha-catenin from the membrane to the c
ytoplasm, Thus, cadherin is required to localize alpha-catenin to the membr
ane, but the amount of alpha-catenin along the membrane seems to be restric
ted to a certain level which cannot be exceeded. The relevance of these obs
ervations for the regulation of cadherin-mediated cell adhesion in the Xeno
pus embryo is discussed. Additionally, we demonstrate that plakoglobin, lik
e beta-catenin an armadillo repeat protein, shows neither accumulation afte
r overexpression nor colocalization with the overexpressed cadherin, Dev Dy
n 1999;215:155-169. (C) 1999 Wiley-Liss, Inc.