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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The 3BP2 Adapter Protein Is Required for Optimal B-Cell Activation and Thymus-Independent Type 2 Humoral Response.

3BP2 is a pleckstrin homology domain- and Src homology 2 (SH2) domain-containing adapter protein that is mutated in the rare human bone disorder cherubism and which has also been implicated in immunoreceptor signaling. However, a function for this protein has yet to be established. Here we show that mice lacking 3BP2 exhibited a perturbation in the peritoneal B1 and splenic marginal-zone B-cell compartments and diminished thymus-independent type 2 antigen response. 3BP2(-/-) B cells demonstrated a proliferation defect in response to antigen receptor cross- linking and a heightened sensitivity to B-cell receptor- induced death via a caspase-3-dependent apoptotic pathway. We show that 3BP2 binds via its SH2 domain to the CD19 signaling complex and is required for optimum Syk phosphorylation and calcium flux.[1]

References

  1. The 3BP2 Adapter Protein Is Required for Optimal B-Cell Activation and Thymus-Independent Type 2 Humoral Response. Chen, G., Dimitriou, I.D., La Rose, J., Ilangumaran, S., Yeh, W.C., Doody, G., Turner, M., Gommerman, J., Rottapel, R. Mol. Cell. Biol. (2007) [Pubmed]
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