By Frederick W. Alt
Advances in Immunology, a usual and hugely revered book, offers present advancements in addition to complete studies in immunology. Articles handle the big variety of issues that include immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and scientific modalities. Edited and authored via the main scientists within the box, each one quantity presents up to date info and instructions for the future.
* Contributions from top experts * Informs and updates on the entire most modern advancements within the box
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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). More structural and biochemical studies are required to elucidate dynamics in the receptor–TRAFs–cIAPs–NIK complex. Unlike canonical NF-κB signaling, deubiquitination is thought to have a positive role in noncanonical NF-κB signaling, although related DUBs and their role are largely unknown.
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).
2014). Therefore, further studies are required to clearly understand the role of linear ubiquitin chains/LUBAC in TNF-α-induced NF-κB activation and control of inflammatory responses. Deubiquitination plays a key role in NF-κB signaling pathways by reversing the effect of ubiquitination. A20 is one of the most well-studied DUBs that contains OTU DUB domain at the N-terminus and Cys2/ Cys2 ZnF E3 ligase domain at the C-terminus, which plays a dual role for RIP1 regulation in TNFR1 signaling (Ma & Malynn, 2012).