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By Frederick W. Alt

Advances in Immunology, a fashioned and hugely revered book, provides present advancements in addition to complete reports in immunology. Articles handle the wide variety of themes that include immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and medical modalities. Edited and authored via the major scientists within the box, every one quantity offers up to date info and instructions for the future.

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* Contributions from prime professionals * Informs and updates on the entire newest advancements within the box

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UBIQUITINATION IN NF-κB SIGNALING The nuclear factor kappa B (NF-κB) family of transcription factors, which consists of p50, p52, p65 (RelA), c-Rel, and RelB, is a key regulator of various cellular processes including immune response, inflammation, and cell survival (Hayden & Ghosh, 2008). The NF-κB family is present in the cytosol bound to inhibitory proteins of κB family (IκB) under nonstimulated conditions. Upon numerous stimuli such as inflammatory cytokines, antigen receptors, and microorganisms, IκB is phosphorylated by IKK complex and subsequently undergoes ubiquitination and proteasomal degradation, which allows NF-κB to translocate to the nucleus from cytosol and regulates the transcription of a variety of target genes.

4. Noncanonical NF-κB signaling: CD40 Engagement of a subset of TNFR family member, CD40 with its ligand CD40L on B cells activates noncanonical NF-κB signaling pathway in a ubiquitin–proteasome-dependent manner. The proteasomal processing of p100 to p52 is the key process of the noncanonical NF-κB signaling, which is mediated by NIK and IKKα. CD40 ligation-induced activation of NIK phosphorylates IKKα, which in turn leads to phosphorylation and subsequent processing of p100 (Sun, 2010a). In steady state, NIK protein level is constitutively regulated by TRAF3-mediated ubiquitination and proteasomal degradation.

However, Th17 cells were induced from Ndfip1À/À mice, even though Ndfip1À/À T cells were not efficient for Th17 differentiation (Ramon, Beal, Liu, Worthen, & Oliver, 2012). The induction of Th17 cells was caused by increasing IL-6-producing eosinophils in lungs from Ndfip1À/À mice, since enhanced Th2 response was able to recruit those eosinophils into lungs. Thus, Th17 cells could be regulated indirectly by Ndfip1À/À T cells. Recently, deubiquitinase USP18 was identified as a regulator in Th17 differentiation.

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