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Keywords {🔍}

mlkl, necroptosis, ripk, cell, article, google, scholar, cas, death, activation, ubiquitination, human, membrane, mouse, cells, phosphorylation, caspase, nature, kinase, fig, ubiquitin, viral, apoptosis, rip, virus, infection, domain, modifications, role, inhibition, authors, signalling, necroptotic, inflammation, killing, induce, activity, signaling, protein, wang, receptors, plasma, independent, host, specific, potential, reported, cellular, necrosis, required,

Topics {✒️}

human k16/r17/k26/q27/k50/r51 nature portfolio privacy policy advertising receptor-interacting kinase-3-mediated pathway scientific journey tlr-myd88-induced ciap1-traf2 degradation german research foundation social media caspase-8-driven il-1beta activation reprints nature immunology tnf-induced nf-kappab signal undergoes multi-mono-ubiquitination cytomegalovirus rip1-interacting protein nature 2015 nature 2018 nature 2011 nature 2019 nature dna sensor zbp1/dai form oligo-multimeric structures caspase-8c362s/c362sripk3−/− mice death-receptor-induced apoptosis cell cycle dependent-manner fadd/ripk1/caspase-8-dependent apoptosis necroptosis-dependent harmful phenotype caspase-8c362s/e-ko tnfr2-traf signaling complex synthesize poly-ubiquitin chains mlkl-induced cellular burst necroptosis-mediated skin damage personal data open questions research viruses including sars-cov-2 tnf-induced inflammatory diseases ripk3-driven cell death multiple lysine-mutant versions mlkl post-translational modifications tnf-r1 signaling complex virus-induced cell death rip3-rip3 homo-interaction cell death-independent manner original author reported post-translational modifications receptor-interacting protein host-induced protective mechanism ubiquitin-modified mlkl enhances ripk1 prevents tradd-driven

Questions {❓}

• Can MLKL induce cell death in a RIPK3 independent manner?
• Do different cellular pools of MLKL exist, whose specific ubiquitination leads to distinct biological outcomes?
• Does MLKL have any physiological role independent of RIPK3 and necroptosis?
• Does mono-ubiquitination vs poly-ubiquitination, and within the latter, the ubiquitin linkage type, differentially control MLKL activity?
• How can ubiquitination differentially regulate MLKL-killing potential?
• What pressure would induce viruses to develop targeting mechanisms also against MLKL?
• Which is/are the E3 ligase(s) and DUB(s) that regulate the conjugation of ubiquitin to, and removal of ubiquitin from, MLKL?
• Why is MLKL controlled by IFN signalling and what is its biological significance?

Schema {🗺️}

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         headline:MLKL post-translational modifications: road signs to infection, inflammation and unknown destinations
         description:Necroptosis is a caspase-independent modality of cell death that requires the activation of the executioner MLKL. In the last ten years the field gained a substantial amount of evidence regarding its involvement in host response to pathogens, TNF-induced inflammatory diseases as well as pathogen recognition receptors (PRR)-induced inflammation. However, there are still a lot of questions that remain unanswered. While it is clear that there are specific events needed to drive MLKL activation, substantial differences between human and mouse MLKL not only highlight different evolutionary pressure, but also provide potential insights on alternative modalities of activation. While in TNF-induced necroptosis it is clear the involvement of the RIPK3 mediated phosphorylation, it still remains to be understood how certain inflammatory in vivo phenotypes are not equally rescued by either RIPK3 or MLKL loss. Moreover, the plethora of different reported phosphorylation events on MLKL, even in cells that do not express RIPK3, suggest indeed that there is more to MLKL than RIPK3-mediated activation, not only in the execution of necroptosis but perhaps in other inflammatory conditions that include IFN response. The recent discovery of MLKL ubiquitination has highlighted a new checkpoint in the regulation of MLKL activation and the somewhat conflicting evidence reported certainly require some untangling. In this review we will highlight the recent findings on MLKL activation and involvement to pathogen response with a specific focus on MLKL post-translational modifications, in particular ubiquitination. This review will highlight the outstanding main questions that have risen from the last ten years of research, trying at the same time to propose potential avenues of research.
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      headline:MLKL post-translational modifications: road signs to infection, inflammation and unknown destinations
      description:Necroptosis is a caspase-independent modality of cell death that requires the activation of the executioner MLKL. In the last ten years the field gained a substantial amount of evidence regarding its involvement in host response to pathogens, TNF-induced inflammatory diseases as well as pathogen recognition receptors (PRR)-induced inflammation. However, there are still a lot of questions that remain unanswered. While it is clear that there are specific events needed to drive MLKL activation, substantial differences between human and mouse MLKL not only highlight different evolutionary pressure, but also provide potential insights on alternative modalities of activation. While in TNF-induced necroptosis it is clear the involvement of the RIPK3 mediated phosphorylation, it still remains to be understood how certain inflammatory in vivo phenotypes are not equally rescued by either RIPK3 or MLKL loss. Moreover, the plethora of different reported phosphorylation events on MLKL, even in cells that do not express RIPK3, suggest indeed that there is more to MLKL than RIPK3-mediated activation, not only in the execution of necroptosis but perhaps in other inflammatory conditions that include IFN response. The recent discovery of MLKL ubiquitination has highlighted a new checkpoint in the regulation of MLKL activation and the somewhat conflicting evidence reported certainly require some untangling. In this review we will highlight the recent findings on MLKL activation and involvement to pathogen response with a specific focus on MLKL post-translational modifications, in particular ubiquitination. This review will highlight the outstanding main questions that have risen from the last ten years of research, trying at the same time to propose potential avenues of research.
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