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Most mature B lymphocytes coexpress two classes of antigen receptor, IgM and IgD. The differences in the signal transduction from the two receptors are still a matter of controversy. We have analyzed B-cell lines expressing IgM or IgD antigen receptors with the same antigen specificity. Cross-linking of these receptors with either antigen or class-specific antibodies results in the activation of protein tyrosine kinases and the phosphorylation of the same substrate proteins. The kinetic and intensity of phosphorylation, however, was quite different between the two receptors when they were cross-linked by antigen. In membrane IgM-expressing cells, the substrate phosphorylation reached a maximum after one minute and diminished after 60 minutes, whereas in the membrane IgD-expressing cells, the substrate phosphorylation increased further over time, reaching its maximum at 60 minutes and persisting longer than 240 minutes after exposure to antigen. Recently prolonged signaling has been found to be responsible for signaling differences between tyrosine kinase receptors using otherwise similar signaling routes. Thus, the duration of a signal may be an important biological feature of signal-transducing cascades.