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- W4313350108 abstract "Abstract B cell memory is critical for the protection from many infectious diseases and is the basis of many current vaccines. Memory B cells expressing high-affinity, IgG-BCRs give rise to the rapid production of high-affinity IgG antibody recall responses, the mechanisms by which the IgG BCRs function to enhance B cell responses are not understood. Studies in mouse models showed that the cytoplasmic tail of membrane-bound IgG (mIgG) is both required and sufficient for the enhanced IgG antibody recall response. Recently, we showed that the conserved membrane proximal region of the mIgG1 cytoplasmic tail, a region not previously appreciated to play a role in BCR signaling, was both necessary and sufficient to dramatically enhance the early events in the initiation of B cell activation. We now identify Dlg1 as a specific, antigen-induced binding partner of the mIgG1 cytoplasmic tail. We demonstrate that Dlg1 and mIg associate through a mechanism involving the binding of the N-terminal and PDZ domains of Dlg1 to the membrane proximal region of the mIgG1 tail. In response to antigens, Dlg1 is rapidly recruited to IgG1-BCR microcluster and then the IgG1-B cell immune synapse. Using live B cell imaging by fluorescence lifetime imaging microscopy we observed that antigen binding induces a molecular complex of Dlg1 and IgG-BCR. Our further evidence suggests that Dlg1 serves as a BCR adaptor stabilizing the formation of IgG-BCR oligomers and facilitating the assembly of signalosome." @default.
- W4313350108 created "2023-01-06" @default.
- W4313350108 creator A5007442731 @default.
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- W4313350108 date "2011-04-01" @default.
- W4313350108 modified "2023-10-01" @default.
- W4313350108 title "Disk large protein 1 promotes the initiation of isotype-switched IgG-BCR signaling (50.15)" @default.
- W4313350108 doi "https://doi.org/10.4049/jimmunol.186.supp.50.15" @default.
- W4313350108 hasPublicationYear "2011" @default.
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