The emergence of pattern in embryogenesis: regulation of beta-catenin localization during early sea urchin development.
The accumulation of beta-catenin in the nuclei of blastomeres at one pole of the early embryo is a highly conserved and essential feature of animal development. In the sea urchin, beta-catenin accumulates in the nuclei of vegetal blastomeres during early cleavage and activates gene regulatory networks that drive mesoderm and endoderm formation. Measurements of beta-catenin half-life in vivo have demonstrated a gradient in stability along the animal-vegetal axis. Dishevelled (Dsh), a protein that regulates beta-catenin turnover, is localized in the vegetal cortex, where it has an essential role in stabilizing beta-catenin and activating endomesodermal gene networks. Two motifs of Dsh are required for targeting to the vegetal cortex. Overexpression of Dsh in animal blastomeres does not alter their fate, which suggests that a localized activator of Dsh may be missing in these cells. Wnt signaling may be localized in the early sea urchin embryo, as it is in Xenopus, but findings point to possible differences in the initial polarizing signal in amphibians and echinoderms. Further studies will be required to determine the extent to which mechanisms that control beta-catenin nuclearization in early embryogenesis have been conserved during animal evolution.
Ettensohn
Charles A
CA
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA. ettensohn@andrew.cmu.edu
D048868:Adaptor Proteins, Signal Transducing / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D000818:Animals; D001757:Blastomeres / Q000378:metabolism; D019521:Body Patterning / Q000235:genetics; D019070:Cell Lineage; D000072261:Dishevelled Proteins; D004625:Embryo, Nonmammalian / Q000648:ultrastructure; D018507:Gene Expression Regulation, Developmental; D009024:Morphogenesis / Q000235:genetics; D010750:Phosphoproteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000235:genetics; D012617:Sea Urchins / Q000196:embryology* / Q000235:genetics; D051153:Wnt Proteins / Q000032:analysis / Q000235:genetics; D029867:Xenopus Proteins / Q000032:analysis / Q000235:genetics; D014982:Xenopus laevis / Q000196:embryology / Q000235:genetics; D051176:beta Catenin / Q000032:analysis / Q000235:genetics / Q000502:physiology*
D048868:Adaptor Proteins, Signal Transducing; C495266:CTNNB1 protein, Xenopus; C000606586:DVL1 protein, Xenopus; D000072261:Dishevelled Proteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D051153:Wnt Proteins; D029867:Xenopus Proteins; D051176:beta Catenin; C512785:wnt11b protein, Xenopus