Fc receptor–like 1 intrinsically recruits c-Abl to enhance B cell activation and function

作者：Xingwang Zhao, Hengyi Xie, Meng Zhao, Asma Ahsan, Xinxin Li, Fei Wang, Junyang Yi, Zhiyong Yang, Chuan Wu, Indu Raman, Quan‐Zhen Li, Tae Jin Kim, Wanli Liu · 发表于：Science Advances · 年份：2019 · DOI：10.1126/sciadv.aaw0315 · 被引用次数：33 · 研究领域：Chronic Myeloid Leukemia Treatments、Monoclonal and Polyclonal Antibodies Research、Mast cells and histamine

ENV 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.