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Letters to Nature

Nature 426, 446-450 (27 November 2003) | doi:10.1038/nature02113; Received 25 June 2003; Accepted 6 October 2003

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An ancient role for nuclear bold beta-catenin in the evolution of axial polarity and germ layer segregation

Athula H. Wikramanayake1, Melanie Hong1,2, Patricia N. Lee2, Kevin Pang2, Christine A. Byrum1, Joanna M. Bince1, Ronghui Xu1 & Mark Q. Martindale2

  1. Department of Zoology, University of Hawaii at Manoa, 2538 McCarthy Mall, Honolulu 96822, Hawaii
  2. Kewalo Marine Lab/Pacific Biomedical Research Center, University of Hawaii, 41 Ahui Street, Honolulu 96813, Hawaii

Correspondence to: Athula H. Wikramanayake1Mark Q. Martindale2 Email: athula@hawaii.edu
Email: mqmartin@hawaii.edu

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The human oncogene beta-catenin is a bifunctional protein with critical roles in both cell adhesion and transcriptional regulation in the Wnt pathway1, 2, 3. Wnt/beta-catenin signalling has been implicated in developmental processes as diverse as elaboration of embryonic polarity2, 3, 4, 5, 6, formation of germ layers4, 5, 6, 7, 8, neural patterning, spindle orientation and gap junction communication2, but the ancestral function of beta-catenin remains unclear. In many animal embryos, activation of beta-catenin signalling occurs in blastomeres that mark the site of gastrulation and endomesoderm formation5, 6, 7, 8, 9, 10, raising the possibility that asymmetric activation of beta-catenin signalling specified embryonic polarity and segregated germ layers in the common ancestor of bilaterally symmetrical animals. To test whether nuclear translocation of beta-catenin is involved in axial identity and/or germ layer formation in 'pre-bilaterians', we examined the in vivo distribution, stability and function of beta-catenin protein in embryos of the sea anemone Nematostella vectensis (Cnidaria, Anthozoa). Here we show that N. vectensis beta-catenin is differentially stabilized along the oral–aboral axis, translocated into nuclei in cells at the site of gastrulation and used to specify entoderm, indicating an evolutionarily ancient role for this protein in early pattern formation.