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

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The RasGAP- binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells.

The low affinity receptor for IgG, FcgammaRIIB, functions to dampen the antibody response and reduce the risk of autoimmunity. This function is reportedly mediated in part by inhibition of B cell antigen receptor (BCR)-mediated p21ras activation, though the basis of this inhibition is unknown. We show here that FcgammaRIIB-BCR coaggregation leads to increased tyrosine phosphorylation of the RasGAP-binding protein p62dok, with a concomitant increase in its binding to RasGAP. These effects require the recruitment and tyrosine phosphorylation of the phosphatidylinositol 5-phosphatase SHIP, which further recruits p62dok via the latter's phosphotyrosine-binding domain. Using chimeric FcgammaRIIB containing the RasGAP-binding domain of p62dok, we demonstrate that p62dok contains all structural information required to mediate the inhibitory effect of FcgammaRIIB on Erk activation.[1]

References

  1. The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells. Tamir, I., Stolpa, J.C., Helgason, C.D., Nakamura, K., Bruhns, P., Daeron, M., Cambier, J.C. Immunity (2000) [Pubmed]
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