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Significance Vertebrate β-catenin has two functions: as a structural component in cell adhesion and as the T-cell factor coactivator in canonical Wnt (wingless-related integration site) signaling. These two functions are split between three β-catenin–related proteins inCaenorhabditis elegans . A fourth worm β-catenin–related protein, worm arm motif 1 (WRM-1), exhibits neither of these functions but is essential, together with loss of intestine 1 (LIT-1) MAPK, for transcriptional activation of Wnt target genes. Here we characterize previously unidentified mechanisms by which the LIT-1 kinase is activated and the different regulatory roles that WRM-1 plays in LIT-1 activation and LIT-1 subcellular localization. This study suggests the potential for novel and as yet undiscovered functions for vertebrate β-catenin.

β-Catenin–related protein WRM-1 is a multifunctional regulatory subunit of the LIT-1 MAPK complex