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* Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, and
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892
The Cbl family of proteins negatively regulate signaling from tyrosine kinase-coupled receptors. Among the three members of this family, only c-Cbl and Cbl-b are expressed in hemopoietic cells. To examine the role of c-Cbl and Cbl-b in Fc
RI signaling, mast cell cultures from wild-type, c-Cbl–/–, and Cbl-b–/– mice were generated. Cell growth rates and cell surface expression of FcRI were similar in the different cell populations. Compared with control cells, Cbl-b inactivation resulted in increases in FcRI-induced Ca2+ response and histamine release. FcRI-induced tyrosine phosphorylation of total cellular proteins, Syk, and phospholipase C-
was also enhanced by Cbl-b deficiency, whereas receptor-initiated phosphorylation of Vav, JNK, and p38 kinases was not changed in these cells. In contrast to Cbl-b, c-Cbl deficiency had no detectable effect on FcRI-induced histamine release or on the phosphorylation of total cellular proteins or Syk. The absence of c-Cbl increased the phosphorylation of ERK after receptor stimulation, but resulted in slightly reduced p38 phosphorylation and Ca2+ response. These results suggest that Cbl-b and c-Cbl have divergent effects on FcRI signal transduction and that Cbl-b, but not c-Cbl, functions as a negative regulator of FcRI-induced degranulation.
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