CELE_C54D1.6, pvl-1, spy-1, C54D1.6

bar-1 encodes a beta-catenin; during C. elegans development, BAR-1 likely functions as a transcriptional coactivator whose activity is required for Q neuroblast migration, P12 cell fate specification, and P3.p through P8.p vulval cell fate specification at two different stages of development; in specifying vulval cell fates, bar-1 interacts with Wnt and MAPK signaling pathways to regulate proper expression of the LIN-39 homeodomain transcription factor, overexpresion of which can partially rescue the bar-1 mutant phenotype; in yeast two-hybrid assays, BAR-1 interacts strongly with the POP-1/TCF transcription factor, and when fused to the Gal4 DNA binding domain, BAR-1 can function in yeast as a transcriptional coactivator; during larval development, BAR-1 expression begins in P3.p through P8.p at the late L1 stage and then disappears from these cells by the mid-L3 stage; BAR-1 is also expressed in P12, in the seam cells, and in cells of the somatic gonad; BAR-1 subcellular localization, assessed using an integrated transgene, reveals localization to the cytoplasm, nucleus, and cell junctions; genetic mosaic analyses indicate that, in P4.p and in P12, bar-1 acts cell autonomously to specify cell fates.

CELE_F52E1.1, F52E1.1

pos-1 encodes a CCCH-type zinc-finger protein; during embryogenesis, maternally provided POS-1 is essential for proper fate specification of germ cells, intestine, pharynx, and hypodermis; POS-1's role in cell fate specification is likely as a translational regulator, as POS-1 is required, in posterior blastomeres, for positive regulation of apx-1 mRNA translation and negative regulation of glp-1 mRNA translation via direct binding to the spatial control region (SCR) in the glp-1 mRNA 3' UTR; in regulating mRNA translation, POS-1 interacts with SPN-4, an RNP-type RNA binding protein, that may function to negatively regulate POS-1 activity; POS-1 can also bind the mex-6 3'-UTR in vitro, although expression of a MEX-6 reporter fusion protein does not appear to be affected in pos-1 mutant animals; pos-1 mRNA is first detected in the gonads of L4 and adult animals, and is present uniformly in oocytes and newly fertilized embryos; during early embryonic divisions, pos-1 mRNA is present at higher levels in germline blastomeres until it disappears following the division of P4; POS-1 protein is first apparent at low levels in 1-cell embryos, with subsequent expression mirroring that of pos-1 mRNA: high levels in germline blastomeres until its disappearance after the P4 division; in the germline blastomeres P1, P2, P3, and P4, POS-1 colocalizes with cytoplasmic and perinuclear P granules.