The constant region of the membrane immunoglobulin mediates B cell-receptor clustering and signaling in response to membrane antigens.

Immunity
Pavel TolarSusan K Pierce

Abstract

B cells are activated in vivo after the B cell receptors (BCRs) bind to antigens captured on the surfaces of antigen-presenting cells. Antigen binding results in BCR microclustering and signaling; however, the molecular nature of the signaling-active BCR clusters is not well understood. Using single-molecule imaging techniques, we provide evidence that within microclusters, the binding of monovalent membrane antigens results in the assembly of immobile signaling-active BCR oligomers. The oligomerization depends on interactions between the membrane-proximal Cmicro4 domains of the membrane immunoglobulin that are both necessary and sufficient for assembly. Antigen-bound BCRs that lacked the Cmicro4 domain failed to cluster and signal, and conversely, Cmicro4 domains alone clustered spontaneously and activated B cells. These results support a unique mechanism for the initiation of BCR signaling in which antigen binding induces a conformational change in the Fc portion of the BCR, revealing an interface that promotes BCR clustering.

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Citations

Jun 15, 2013·Journal of the American Chemical Society·Anna GrochmalSalvador Tomas
Dec 17, 2009·The Journal of Physical Chemistry. B·A Srinivas ReddySubhadip Raychaudhuri
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Apr 21, 2010·The Journal of Experimental Medicine·Wanli LiuSusan K Pierce
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