| First Author | Tamir I | Year | 2000 |
| Journal | Immunity | Volume | 12 |
| Issue | 3 | Pages | 347-58 |
| PubMed ID | 10755621 | Mgi Jnum | J:112435 |
| Mgi Id | MGI:3656333 | Doi | 10.1016/s1074-7613(00)80187-9 |
| Citation | Tamir I, et al. (2000) The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells. Immunity 12(3):347-58 |
| abstractText | 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. |
