CTX, a new Xenopus Ig superfamily molecule present on some cortical thymocytes and lymphoid tumor cells, is expressed at the cell surface under six differently glycosylated isoforms as shown by two-dimensional gel analysis and by endo F glycosidase treatment. Following chemical cross-linking before immunoprecipitation, a large fraction of surface CTX forms non-covalently linked dimers at the cell surface. This finding, which is consistent with the presence of a J segment with diglycine beta bulge in the V region of the molecule, suggests that this dimer has the same conformation as a T-cell receptor (TCR) or an Ig molecule. The V8 digest patterns of the monomers and dimers are identical. While this suggests that the dimer is a homodimer of two CTX chains, it does not distinguish whether each CTX chain is encoded by the same or different gene loci. When tumor cells were added to culture wells that had been coated with the anti-CTX monoclonal antibody X71, 30-50% underwent rapid (within 30 min) morphological changes followed by growth inhibition as determined by a decrease in thymidine incorporation and by direct cell counting. No apoptosis, calcium flux or external calcium requirement was noted after cross-linking of CTX. These results suggest that CTX can function as a receptor, and that its interaction with a ligand influences the control of cell proliferation through a signalling pathway that is distinct from the TCR machinery.