By Frederick W. Alt
Advances in Immunology, a usual and hugely revered e-book, provides present advancements in addition to finished experiences in immunology. Articles deal with the big variety of issues that contain immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and scientific modalities. Edited and authored via the key scientists within the box, every one quantity presents up to date info and instructions for the future.
* Contributions from best experts * Informs and updates on the entire most recent advancements within the box
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Extra resources for Advances in Immunology
Most Tregs express Foxp3, a master transcription factor, which is crucial for their suppressive activities. It has been studied that several E3 ubiquitin ligases regulate the differentiation and/or the function of Treg. One of the E3 ubiquitin ligases, GRAIL, is responsible for Treg function. , 2009). , 2010). Tregs are classified into two distinct populations: one is naturally occurring Treg (nTreg) generated in thymus and another is induced Treg (iTreg) developed in periphery. Both Treg subtypes shared many common features in function and expression of Treg markers.
CYLD has been known to negatively regulate NF-κB activation in TCR signaling by removing K63-linked polyubiquitin chains from TAK1. , 2007). We recently reported that USP9X DUB plays a positive role for TCR-induced NF-κB activation via facilitating CBM complex formation (Park, Jin, & Liu, 2013). As there is still a lack of knowledge of DUBs that possibly play a crucial role in TCR-induced NF-κB signaling, future studies will be required to characterize and establish the role of DUBs. 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.
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.