http://www.jbc.org/content/288/43/31268.full.pdf

Toll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKL

Innate immunity represents the first line of defence against invading pathogens. It consists of an initial inflammatory response that recruits white blood cells to the site of infection in an effort to destroy and eliminate the pathogen. Some pathogens replicate within host cells, and cell death by apoptosis is an important effector mechanism to remove the replication niche for such microbes. However, some microbes have evolved evasive strategies to block apoptosis, and in these cases host cells may employ further countermeasures, including an inflammatory form of cell death know as necroptosis. This review aims to highlight the importance of the RIP kinase family in controlling these various defence strategies. RIP1 is initially discussed as a key component of death receptor signalling and in the context of dictating whether a cell triggers a pathway of pro-inflammatory gene expression or cell death by apoptosis. The molecular and functional interplay of RIP1 and RIP3 is described, especially with respect to mediating necroptosis and as key mediators of inflammation. The function of RIP2, with particular emphasis on its role in NOD signalling, is also explored. Special attention is given to emphasizing the physiological and pathophysiological contexts for these various functions of RIP kinases.

/pdf/rip-kinases-key-decision-makers-in-cell-death-and-innate-4qntrts5j3.pdf

RIP kinases: key decision makers in cell death and innate immunity

https://www.gastrojournal.org/article/S0016-5085(10)01320-X/pdf

The Spectrum of Achalasia: Lessons From Studies of Pathophysiology and High-Resolution Manometry

Apoptosis and Necroptosis as Host Defense Strategies to Prevent Viral Infection

Ubiquitination is a post-translational modification process that has been implicated in the regulation of innate and adaptive immune responses. There is increasing evidence that both ubiquitination and its reversal, deubiquitination, play crucial roles not only during the development of the immune system but also in the orchestration of an immune response by ensuring the proper functioning of the different cell types that constitute the immune system. Here, we provide an overview of the latest discoveries in this field and discuss how they impact our understanding of the ubiquitin system in host defence mechanisms as well as self-tolerance.

https://www.embopress.org/doi/pdf/10.1002/embr.201338025

Ubiquitin in the immune system

Toll-like receptor 3 (TLR3) is a pattern-recognition receptor known to initiate an innate immune response when stimulated by double-stranded RNA (dsRNA). Components of TLR3 signaling, including TIR domain-containing adapter inducing IFN-α (TRIF), have been demonstrated to contribute to dsRNA-induced cell death through caspase-8 and receptor interacting protein (RIP)1 in various human cancer cells. We provide here a detailed analysis of the caspase-8 activating machinery triggered in response to Poly(I:C) dsRNA. Engagement of TLR3 by dsRNA in both type I and type II lung cancer cells induces the formation of an atypical caspase-8-containing complex that is devoid of classical death receptors of the TNFR superfamily, but instead is physically associated to TLR3. The recruitment of caspase-8 to TLR3 requires RIP1, and is negatively modulated by cellular inhibitor of apoptosis protein (cIAP)2–TNF receptor-associated factor (TRAF)2–TNFR-associated death domain (TRADD) ubiquitin ligase complex, which regulates RIP1 ubiquitination. Intriguingly, unlike Fas- or TRAILR-dependent death signaling, caspase-8 recruitment and activation within the TLR3 death-signaling complex appears not to be stringently dependent on Fas-associated with death domain (FADD). Our findings uncover a novel aspect of the molecular mechanisms involved during apoptosis induced by the innate immune receptor TLR3 in cancer cells.

/pdf/dsrna-induces-apoptosis-through-an-atypical-death-complex-4tl4r6ileb.pdf

dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8.

/pdf/tlr3-maturation-localisation-and-apoptotic-role-in-cancer-1dydzheg4y.pdf

Tlr3 maturation, localisation and apoptotic role in cancer.

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dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8.

Tlr3 maturation, localisation and apoptotic role in cancer.