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Wnts are a conserved family of secreted glycoproteins that regulate various developmental processes in metazoans. Three of the five Caenorhabditis elegans Wnts, CWN-1, CWN-2 and EGL-20, and the sole Wnt receptor of the Ror kinase family, CAM-1, are known to regulate the anterior polarization of the mechanosensory neuron ALM. Here we show that CAM-1 and the Frizzled receptor MOM-5 act in parallel pathways to control ALM polarity. We also show that CAM-1 has two functions in this process: an autonomous signaling function that promotes anterior polarization and a nonautonomous Wnt-antagonistic function that inhibits anterior polarization. These antagonistic activities can account for the weak ALM phenotypes displayed by cam-1 mutants. Our observations suggest that CAM-1 could function as a Wnt receptor in many developmental processes, but the analysis of cam-1 mutants may fail to reveal CAM-1's role as a receptor in these processes because of its Wnt-antagonistic activity. In this model, loss of CAM-1 results in increased levels of Wnts that act through other Wnt receptors, masking CAM-1's autonomous role as a Wnt receptor.
cam-1 encodes a Caenorhabditis elegans orphan receptor tyrosine kinase (RTK) of the Ror family that is required for cell migration and to orient cell polarity. Ror RTKs share a common domain structure. The predicted extracellular region contains immunoglobulin (Ig), cysteine-rich (CRD), and kringle (Kri) domains. Intracellularly are tyrosine kinase (Kin) and serine- and threonine (S/T)-rich domains. To investigate the functional requirement for CAM-1 domains in mediating cell migration, we engineered deletions that remove various domains and assessed the ability of these CAM-1 derivatives to rescue cam-1 mutant phenotypes. We find that the Ig, Kri, Kin, and S/T domains are dispensable for cell migration, but the CRD is required. Surprisingly, the entire intracellular region of CAM-1 is not required for proper cell migration. Most notably, a version of CAM-1 from which all domains besides the CRD and transmembrane domains have been deleted is able to rescue the migration of a single cell type, although not those of other cell types. Our results show that CAM-1 does not function exclusively as a canonical RTK and that it may function, at least in part, to regulate the distribution of a secreted ligand-possibly a Wnt protein.
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