Annual Review of Immunology Volume 28 2010 by Annual Reviews

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Indeed, the overexpression of IRF4 in an IRF4−/− IRF8−/− background resulted in high levels of Igκ germline transcripts and preferentially stimulated histone H4 acetylation at the 3 Eκ. In contrast, lowering the IL-7 signaling preferentially induces histone acetylation at the iEκ (169). Although the mechanisms are not entirely clear, the lowered IL-7 signaling appears to facilitate binding of the transcription factor E2A to the iEκ, which in turn is required for Igκ recombination in pre-B cells.

Similarly, in humans, defective CD40L expression results in the X-linked form of hyper IgM syndrome. B cells in these patients are unable to undergo Ig class switching due to the lack of the CD40L-CD40 interaction. In vitro, the ligation of CD40 on B cells stimulates their survival, proliferation, and differentiation; promotes Ig isotype switching; and induces the upregulation of surface molecules involved in antigen presentation. The CD40-associated TRAF2, TRAF3, and TRAF6 initiate the NF-κB (both canonical and noncanonical), JNK, and p38 pathways (213, 214).

In this setting, B cells can recognize DNAor RNA-containing antigens through their cell surface BCRs, which in turn deliver the DNA/RNA ligands to TLR9/7-containing compartments (132, 133). In this scenario, the BCR functions as a transfer vehicle for inducing TLR9/7 signaling. Thus, BCR internalization can affect several distinct signaling outcomes. 14 C E I N A D V A N Kurosaki · Shinohara · Baba through BCR and targeting into multivesicular late endosomes (alternatively named MHC class II–containing endosomes), presumably through early endosomes; (b) MHC class II complexes, proteases, and H2-DM convergence toward this incoming pool of antigenBCR complexes; and (c) the export of MHC class II–peptide complexes to the cell surface (Figure 4) (129).

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