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

Athula H. Wikramanayake (), Melanie Hong, Patricia N. Lee, Kevin Pang, Christine A. Byrum, Joanna M. Bince, Ronghui Xu and Mark Q. Martindale ()
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Athula H. Wikramanayake: University of Hawaii at Manoa
Melanie Hong: University of Hawaii at Manoa
Patricia N. Lee: University of Hawaii
Kevin Pang: University of Hawaii
Christine A. Byrum: University of Hawaii at Manoa
Joanna M. Bince: University of Hawaii at Manoa
Ronghui Xu: University of Hawaii at Manoa
Mark Q. Martindale: University of Hawaii

Nature, 2003, vol. 426, issue 6965, 446-450

Abstract: Abstract The human oncogene β-catenin is a bifunctional protein with critical roles in both cell adhesion and transcriptional regulation in the Wnt pathway1,2,3. Wnt/β-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 β-catenin remains unclear. In many animal embryos, activation of β-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 β-catenin signalling specified embryonic polarity and segregated germ layers in the common ancestor of bilaterally symmetrical animals. To test whether nuclear translocation of β-catenin is involved in axial identity and/or germ layer formation in ‘pre-bilaterians’, we examined the in vivo distribution, stability and function of β-catenin protein in embryos of the sea anemone Nematostella vectensis (Cnidaria, Anthozoa). Here we show that N. vectensis β-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.

Date: 2003
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DOI: 10.1038/nature02113

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