Annual Reviews's Annual Review of Immunology Volume 28 2010 PDF

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The BAFFR has only a single TRAF-binding site, which is specific for TRAF3 (190). Unlike other TRAFs (such as TRAF2, TRAF5, and TRAF6), TRAF3 does not activate the canonical NFκB or JNK pathway (191). Instead, TRAF3, in the resting state, suppresses the noncanonical NF-κB pathway by binding NIK and targeting it for proteosomal degradation (192). NIK is responsible for directly phosphorylating and activating IKKα and the subsequent activation of the noncanonical pathway (193, 194). Activated BAFFR recruits TRAF3, allowing B cells to terminate TRAF3-mediated degradation of NIK.

The requirement for IL-7 in VH (D)JH recombination fits well with recent observations that pro-B cells are in contact with IL-7-expressing stromal cells in bone marrow microenvironments. In bone marrow, several types of stromal cells (at least three types: osteoblasts, CXCL12hi reticular cells, and IL-7-expressing cells) have been proposed to function as specific cellular niches for promoting early B cell development in a stepwise manner (Figure 5b) (144). Most pre-pro-B cells are in contact with CXCL12hi reticular cells, whereas pro-B cells move away from CXCL12hi reticular cells and instead associate with IL-7-expressing stromal cells.

Nuclear factor of activated T cells (NFAT) is a well-studied calcium-dependent transcription factor downstream of calcineurin (67). NFAT is a cytosolic protein and requires a continuous increase in Ca2+ to remain in the nucleus, wherein it activates transcription of target genes. B cells express three NFAT family members, NFATc1 (alternatively named NFAT2 or NFATc), NFATc2 (NFAT1 or NFATp), and NFATc3 (NFAT4 or NFATx) (68), which are components of the BCR signaling cascade. Although mice deficient in each NFAT member have been reported (69–71), these reports have not addressed the B cell–intrinsic phenotype caused by NFAT inactivation.

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