Congratulations to the Martindale Lab and colleagues whose publication “β-Catenin localization in the ctenophore Mnemiopsis leidyi suggests an ancestral role in cell adhesion and nuclear function" is in the journal Developmental Dynamics.
β-catenin is a structurally and functionally highly conserved protein in the animal kingdom. It is an extensively studied protein due to its dual function inside the cell as a transcriptional co-factor in the Wnt/β-catenin signaling pathway, and a structural component of the Cadherin-Catenin-Complex involved in cell-to-cell adhesion.
Currently, most of our knowledge about this protein is coming from non-bilaterian and cnidarian model organisms. However, β-catenin is poorly characterized in the most ancient metazoan lineage, the ctenophores.
To study this protein in the ctenophore species Mnemiopsis leidyi, Lucas Guttieres, Mayline Goëb and Mark Martindale with their collaborators at the University of Miami generated an antibody specifically targeting β-catenin in M. leidyi.
Their research showed that β-catenin is localized at the cell-cell junctions during M. leidyi embryonic development, which suggests that the role of β-catenin in cell-to-cell adhesion is conserved in M. leidyi. Additionally, initial analyses indicate nuclear translocation of β-catenin, but no relationship to any particular cell lineages have been determined yet for M. leidyi.