| First Author | Castello A | Year | 2013 |
| Journal | Nat Immunol | Volume | 14 |
| Issue | 9 | Pages | 966-75 |
| PubMed ID | 23913047 | Mgi Jnum | J:208233 |
| Mgi Id | MGI:5562509 | Doi | 10.1038/ni.2685 |
| Citation | Castello A, et al. (2013) Nck-mediated recruitment of BCAP to the BCR regulates the PI(3)K-Akt pathway in B cells. Nat Immunol 14(9):966-75 |
| abstractText | The adaptor Nck links receptor signaling to cytoskeleton regulation. Here we found that Nck also controlled the phosphatidylinositol-3-OH kinase (PI(3)K)-kinase Akt pathway by recruiting the adaptor BCAP after activation of B cells. Nck bound directly to the B cell antigen receptor (BCR) via the non-immunoreceptor tyrosine-based activation motif (ITAM) phosphorylated tyrosine residue at position 204 in the tail of the immunoglobulin-alpha component. Genetic ablation of Nck resulted in defective BCR signaling, which led to hampered survival and proliferation of B cells in vivo. Indeed, antibody responses in Nck-deficient mice were also considerably impaired. Thus, we demonstrate a previously unknown adaptor function for Nck in recruiting BCAP to sites of BCR signaling and thereby modulating the PI(3)K-Akt pathway in B cells. |
