By Frederick W. Alt
Advances in Immunology, a normal and hugely revered book, provides present advancements in addition to accomplished stories in immunology. Articles handle the big variety of subject matters that include immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and medical modalities. Edited and authored by means of the key scientists within the box, each one quantity offers updated details and instructions for the future.
* Contributions from prime experts * Informs and updates on the entire most recent advancements within the box
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Additional info for Advances in Immunology
2007). Therefore, more studies are needed to define the precise mechanism of Ubc13/Uev1A–TRAF6-mediated regulation of IL-1R/TLR4 signaling, and thus, characterization of alternate E2–E3 enzymes, which may play an essential role in this pathway, is also needed. , 2009), although it is not clear whether there is a functional redundancy between K63-linked and linear polyubiquitin chains. A more recent study by Emmerich et al. (2013) proposes that K63-linked and linear ubiquitin chains cooperatively work together to modify the signaling molecules in IL-1R/TLR4 pathway including MyD88 and IRAK4 through assembling either K63-linked/linear hybrid ubiquitin chains or interaction between same proteins.
In a cell-free system, oligomerization of TRAF6 is induced by oligomeric forms of BCL10 and MALT1, which activates E3 ligase activity of TRAF6 for NEMO ubiquitination (Sun, Deng, Ea, Xia, & Chen, 2004). , 2007; Wu & Ashwell, 2008). , 2006). , 2004). Ubc13/Uev1A has been thought to play an important role for NF-κB activation in TCR signaling by catalyzing K63-linked polyubiquitin chains with TRAF6, which in turn activates TAK1 and IKK. , 2004). 4 See legend on next page 44 Yoon Park et al. , 2006).
Upon CD40 stimulation, TRAF3 recruits both TRAF2 and the associated cIAP1/2 to the receptor and then TRAF2 catalyzes K63linked polyubiquitin chains on cIAP1/2. Modified cIAP1/2 with K63linked ubiquitin facilitates K48-linked polyubiquitination of TRAF3, which results in proteasomal degradation. , 2008). A recent study proposes an “allosteric regulation model” for the mechanism of NIK stabilization in LTβR signaling that activates noncanonical NF-κB signaling in stromal cells, which suggests that LTβR plays as an allosteric regulator between NIK and TRAFs by competitive binding (Sanjo, Zajonc, Braden, Norris, & Ware, 2010).