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The Journal of Immunology, 2004, 173: 1811-1818.
Copyright © 2004 by The American Association of Immunologists

Inactivation of c-Cbl or Cbl-b Differentially Affects Signaling from the High Affinity IgE Receptor

Juan Zhang1,*, Yungping J. Chiang1,{dagger}, Richard J. Hodes{dagger} and Reuben P. Siraganian2,*

* Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, and {dagger} 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{epsilon}RI signaling, mast cell cultures from wild-type, c-Cbl–/–, and Cbl-b–/– mice were generated. Cell growth rates and cell surface expression of Fc{epsilon}RI were similar in the different cell populations. Compared with control cells, Cbl-b inactivation resulted in increases in Fc{epsilon}RI-induced Ca2+ response and histamine release. Fc{epsilon}RI-induced tyrosine phosphorylation of total cellular proteins, Syk, and phospholipase C-{gamma} 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 Fc{epsilon}RI-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 Fc{epsilon}RI signal transduction and that Cbl-b, but not c-Cbl, functions as a negative regulator of Fc{epsilon}RI-induced degranulation.




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