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Extra info for Annual Review of Immunology Volume 28 2010
These two pathways act via distinct mechanisms to regulate such processes. The Igκ locus contains two distinct transcriptional enhancers, the intronic enhancer (iEκ) and the 3 enhancer (3 Eκ), which function to regulate recombination. 1, it interacts with the 3 Eκ (164, 168). Increased binding of these proteins to the 3 Eκ is associated with its increased accessibility to restriction endonucleases, as well as increased association with acetylated histones in B cells. 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.
STIM1 contains several conserved domains, including the EF-hand motif, sterile α motif (SAM), and coiled-coil domains. In resting B cells, STIM1 looks to move dynamically in a tubulovesicular way on the ER, along with microtubules (57). This behavior is mediated through the coiled-coil domain and Ser/Thrrich C-terminal region, which are located in the cytosolic side. After BCR-induced store depletion, Ca2+ dissociates from the EF-hand motif located in the ER lumen, which may result in R Annu. Rev.
Indeed, B cells that lack TRAF3 show greatly elevated levels of NIK and NF-κB2 processing (195). More signiﬁcantly, the B cell developmental defect in BAFF −/− mice was corrected by the loss of TRAF3, formally demonstrating the importance of the BAFFR-TRAF3-noncanonical NF-κB pathway in the development of mature B cells. TRAF3-mediated NIK degradation is likely mediated by the TRAF2-associated Ub ligase c-IAP1, although how TRAF3 regulates TRAF2 is not clear. In this context, TRAF2, TRAF3, and c-IAP1 function as suppressors of the noncanonical NF-κB pathway in B cells (196).
Annual Review of Immunology Volume 28 2010 by Annual Reviews