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We began analyzing https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0076841, but it redirected us to https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0076841. The analysis below is for the second page.
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BackgroundNecroptosis/programmed necrosis is initiated by a macro-molecular protein complex termed the necrosome. Receptor interacting protein kinase 1 (RIPK1/RIP1) and RIP3 are key components of the necrosome. TNFα is a prototypic inducer of necrosome activation, and it is widely believed that deubiquitination of RIP1 at the TNFR-1 signaling complex precedes transition of RIP1 into the cytosol where it forms the RIP1-RIP3 necrosome. Cylindromatosis (CYLD) is believed to promote programmed necrosis by facilitating RIP1 deubiquitination at this membrane receptor complex. Methodology/Principal FindingsWe demonstrate that RIP1 is indeed the primary target of CYLD in TNFα-induced programmed necrosis. We observed that CYLD does not regulate RIP1 ubiquitination at the TNF receptor. TNF and zVAD-induced programmed necrosis was highly attenuated in CYLD-/- cells. However, in the presence of cycloheximide or SMAC mimetics, programmed necrosis was only moderately reduced in CYLD-/- cells. Under the latter conditions, RIP1-RIP3 necrosome formation is only delayed, but not abolished in CYLD-/- cells. We further demonstrate that RIP1 within the NP-40 insoluble necrosome is ubiquitinated and that CYLD regulates RIP1 ubiquitination in this compartment. Hence, RIP1 ubiquitination in this late-forming complex is greatly increased in CYLD-/- cells. Increased RIP1 ubiquitination impairs RIP1 and RIP3 phosphorylation, a signature of kinase activation. Conclusions/SignificanceOur results show that CYLD regulates RIP1 ubiquitination in the TNFα-induced necrosome, but not in the TNFR-1 signaling complex. In cells sensitized to programmed necrosis with SMAC mimetics, CYLD is not essential for necrosome assembly. Since SMAC mimetics induces the loss of the E3 ligases cIAP1 and cIAP2, reduced RIP1 ubiquitination could lead to reduced requirement for CYLD to remove ubiquitin chains from RIP1 in the TNFR-1 complex. As increased RIP1 ubiquitination in the necrosome correlates with impaired RIP1 and RIP3 phosphorylation and function, these results suggest that CYLD controls RIP1 kinase activity during necrosome assembly.
Title[redir]:
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Description:
BackgroundNecroptosis/programmed necrosis is initiated by a macro-molecular protein complex termed the necrosome. Receptor interacting protein kinase 1 (RIPK1/RIP1) and RIP3 are key components of the necrosome. TNFα is a prototypic inducer of necrosome activation, and it is widely believed that deubiquitination of RIP1 at the TNFR-1 signaling complex precedes transition of RIP1 into the cytosol where it forms the RIP1-RIP3 necrosome. Cylindromatosis (CYLD) is believed to promote programmed necrosis by facilitating RIP1 deubiquitination at this membrane receptor complex. Methodology/Principal FindingsWe demonstrate that RIP1 is indeed the primary target of CYLD in TNFα-induced programmed necrosis. We observed that CYLD does not regulate RIP1 ubiquitination at the TNF receptor. TNF and zVAD-induced programmed necrosis was highly attenuated in CYLD-/- cells. However, in the presence of cycloheximide or SMAC mimetics, programmed necrosis was only moderately reduced in CYLD-/- cells. Under the latter conditions, RIP1-RIP3 necrosome formation is only delayed, but not abolished in CYLD-/- cells. We further demonstrate that RIP1 within the NP-40 insoluble necrosome is ubiquitinated and that CYLD regulates RIP1 ubiquitination in this compartment. Hence, RIP1 ubiquitination in this late-forming complex is greatly increased in CYLD-/- cells. Increased RIP1 ubiquitination impairs RIP1 and RIP3 phosphorylation, a signature of kinase activation. Conclusions/SignificanceOur results show that CYLD regulates RIP1 ubiquitination in the TNFα-induced necrosome, but not in the TNFR-1 signaling complex. In cells sensitized to programmed necrosis with SMAC mimetics, CYLD is not essential for necrosome assembly. Since SMAC mimetics induces the loss of the E3 ligases cIAP1 and cIAP2, reduced RIP1 ubiquitination could lead to reduced requirement for CYLD to remove ubiquitin chains from RIP1 in the TNFR-1 complex. As increased RIP1 ubiquitination in the necrosome correlates with impaired RIP1 and RIP3 phosphorylation and function, these results suggest that CYLD controls RIP1 kinase activity during necrosome assembly.
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Keywords {🔍}
rip, cyld, necrosis, cells, figure, cell, tnf, necrosome, article, view, ubiquitination, google, scholar, complex, programmed, pubmed, tnfr, mefs, kinase, signaling, death, tnfinduced, apoptosis, insoluble, treated, activity, image, activation, plos, caspase, zvadfmk, determined, lanes, western, fractions, riprip, sirna, fadd, sds, results, smac, assembly, blot, protein, regulates, phosphorylation, ubiquitin, expression, chx, zvad,
Topics {✒️}
small interference rnas cookies plos plos nf-kappab-independent cell-death switch medicine open-access article distributed trauma-induced tissue injury original author inflammatory diseases necrotic cell injury induce tnfalpha-dependent apoptosis reactive oxygen species caspase-independent apoptosis pathway rip1-k377r-gfp mutant receptor-interacting protein rip1-dependent necrosis occurs tnfα-induced programmed necrosis fadd-deficient jurkat cells tnf-induced rip1-rip3 necrosome facilitate tnf-induced necrosis membrane-bound tnfr-1 complex membrane-anchored tnfr-1 complex decreased tnf-induced necrosis zvad-induced programmed necrosis tnfalpha-dependent apoptosis death domain protein nf-kappab signaling hiperfect transfection reagent similar rip1-independent necrosis specific immunoprecipitation antibodies thermoscientific/open biosystems phosphatase inhibitor cocktail gfp-tagged cyld mutants nf-kappab activation performed sequential immunoprecipitation rpmi1640 media ordered cellular explosion k63-specific ubiquitin antibodies membrane receptor complex comments complete protease inhibitors ligand-dependent manner acknowledgments references 1 phosphorylation-driven assembly poly-ubiquitinated proteins late-forming complex necrosis signaling pathway tnf-induced necroptosis prevents skin inflammation
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