| First Author | Zhao X | Year | 2019 |
| Journal | Sci Adv | Volume | 5 |
| Issue | 7 | Pages | eaaw0315 |
| PubMed ID | 31328160 | Mgi Jnum | J:293654 |
| Mgi Id | MGI:6453156 | Doi | 10.1126/sciadv.aaw0315 |
| Citation | Zhao X, et al. (2019) Fc receptor-like 1 intrinsically recruits c-Abl to enhance B cell activation and function. Sci Adv 5(7):eaaw0315 |
| abstractText | B cell activation is regulated by the stimulatory or inhibitory co-receptors of B cell receptors (BCRs). Here, we investigated the signaling mechanism of Fc receptor-like 1 (FcRL1), a newly identified BCR co-receptor. FcRL1 was passively recruited into B cell immunological synapses upon BCR engagement in the absence of FcRL1 cross-linking, suggesting that FcRL1 may intrinsically regulate B cell activation and function. BCR cross-linking alone led to the phosphorylation of the intracellular Y281ENV motif of FcRL1 to provide a docking site for c-Abl, an SH2 domain-containing kinase. The FcRL1 and c-Abl signaling module, in turn, potently augmented B cell activation and proliferation. FcRL1-deficient mice exhibited markedly impaired formation of extrafollicular plasmablasts and germinal centers, along with decreased antibody production upon antigen stimulation. These findings reveal a critical BCR signal-enhancing function of FcRL1 through its intrinsic recruitment to B cell immunological synapses and subsequent recruitment of c-Abl upon BCR cross-linking. |
