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Extra info for Annual Review of Immunology Volume 28 2010

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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).

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Annual Review of Immunology Volume 28 2010 by Annual Reviews


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