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Extra info for Annual Review of Immunology Volume 28 2010
The recruitment of Act1 to the BAFFR-TRAF3 complex may provide the negative signal for subsequent NIK activation. In contrast to Act1’s involvement in both CD40 and BAFFR signaling, BANK plays a negative role only in CD40 signaling, presumably through the inhibition of CD40-mediated Akt activation (217). In B cells, Bcl6 is a master regulator of GC commitment, maintenance, and suppression of PC differentiation (212, 218). Thus, it is important to clarify when and how Bcl6 is turned on and off. However, these questions have not yet been adequately addressed.
Indeed, CYLD deﬁciency in B cells results in the constitutive activation of the canonical NF-κB pathway, leading to an enlarged B cell compartment (117, 118). The B cell targets of CYLD are unknown, but based on T cell data, it seems reasonable to propose that the K63 ubiquitylation of IKKγ and TAK1, both of which are critical for IKK activation in BCR signaling context, is a likely candidate. Because the Ser residues in the activation loop of IKKα and IKKβ are not in the context of a PKCβ consensus phosphorylation site, it has been thought that PKCβ mediates phosphorylation of IKK indirectly through an intermediate kinase, which then directly phosphorylates the Ser residues on IKKα/IKKβ.
MHC class II molecules associate with their chaperone molecule invariant chain (li) in the ER. In the antigen-processing late-endosomal compartment, the antigen and li are proteolyzed. The cysteine protease CatS is speciﬁcally required for a late step of li cleavage and allows for peptide exchange by H2-DM. By removing the cytosolic tail of li, this proteolytic event liberates the li motif for endosomal retention and permits mature peptide complexes (pMHC) to be exported to the cell surface for interaction with cognate T cells.
Annual Review of Immunology Volume 28 2010 by Annual Reviews