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Title:
Distinct roles of RIP1–RIP3 hetero- and RIP3–RIP3 homo-interaction in mediating necroptosis | Cell Death & Differentiation
Description:
Necroptosis is mediated by a signaling complex called necrosome, containing receptor-interacting protein (RIP)1, RIP3, and mixed-lineage kinase domain-like (MLKL). It is known that RIP1 and RIP3 form heterodimeric filamentous scaffold in necrosomes through their RIP homotypic interaction motif (RHIM) domain-mediated oligomerization, but the signaling events based on this scaffold has not been fully addressed. By using inducible dimer systems we found that RIP1–RIP1 interaction is dispensable for necroptosis; RIP1–RIP3 interaction is required for necroptosis signaling, but there is no necroptosis if no additional RIP3 protein is recruited to the RIP1–RIP3 heterodimer, and the interaction with RIP1 promotes the RIP3 to recruit other RIP3; RIP3–RIP3 interaction is required for necroptosis and RIP3–RIP3 dimerization is sufficient to induce necroptosis; and RIP3 dimer-induced necroptosis requires MLKL. We further show that RIP3 oligomer is not more potent than RIP3 dimer in triggering necroptosis, suggesting that RIP3 homo-interaction in the complex, rather than whether RIP3 has formed homo polymer, is important for necroptosis. RIP3 dimerization leads to RIP3 intramolecule autophosphorylation, which is required for the recruitment of MLKL. Interestingly, phosphorylation of one of RIP3 in the dimer is sufficient to induce necroptosis. As RIP1–RIP3 heterodimer itself cannot induce necroptosis, the RIP1–RIP3 heterodimeric amyloid fibril is unlikely to directly propagate necroptosis. We propose that the signaling events after the RIP1–RIP3 amyloid complex assembly are the recruitment of free RIP3 by the RIP3 in the amyloid scaffold followed by autophosphorylation of RIP3 and subsequent recruitment of MLKL by RIP3 to execute necroptosis.
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Keywords {🔍}
rip, necroptosis, cell, figure, cells, article, riprip, google, scholar, cas, death, complex, mut, interaction, mlkl, rhim, signaling, domain, kinase, protein, necrosis, dimerization, nature, riprhim, necrosome, dimer, proteins, data, apoptosis, western, scaffold, required, heterodimer, amyloid, autophosphorylation, phosphorylation, antibody, supplementary, usa, recruitment, induced, caspase, apinduced, min, induce, lysates, blotting, size, treated, analysis,
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pan-caspase inhibitor z-val-ala-dl-asp-fluoromethylketone z-val-ala-dl-asp-fluoromethylketone dss open research fund nature portfolio permissions reprints privacy policy advertising open fresh perspectives flag-tagged full-length rip1 tech research social media benzyloxycarbonyl-val-ala-aspfluoromethylketone ha-fkbp-tagged rip3rhim mut flag-frb-rip3rhim mut dimers expressed flag-frb-rip3rhim mut ap21967-induced fkbp-rip3rhim mut nature 2011 nature 2013 nature immunoprecipitated flag-frb-rip3rhim mut rip1rhim mut-rip3wt-induced necroptosis rip1–rip3 signalling hub expressed flag-rfp-tagged dd tnf-induced rip1/rip3 complex full-length rip1 leads rip1rhim mut-rip3rhim mut ap21967-induced rip1–rip3 complex ap21976-induced cell death frb-tagged rip3rhim mut pkc-mapks-ap-1 pathway rip3-driven regulated necrosis cross-linked flag-frb-rip3 divergent nucleotide-binding mechanisms caspase-dependent cell death flag-frb-rip3rhim mut anti-flag antibody shows renal ischemia/reperfusion injury frb-rip3rhim mut complex dai/zbp1 recruits rip1 mixed-lineage kinase domain mixed-linage kinase domain ha-fkbp-rip3rhim mut frb-rip3rhim mut interaction expressed frb-rip3rhim mut rip3-mediated macrophage necrosis mouse anti-β-actin c-terminus-mediated dimerization mlkl post-translational modifications ap21967-induced cell death rip1rhim mut-rip3wt complex
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headline:Distinct roles of RIP1âRIP3 hetero- and RIP3âRIP3 homo-interaction in mediating necroptosis
description:Necroptosis is mediated by a signaling complex called necrosome, containing receptor-interacting protein (RIP)1, RIP3, and mixed-lineage kinase domain-like (MLKL). It is known that RIP1 and RIP3 form heterodimeric filamentous scaffold in necrosomes through their RIP homotypic interaction motif (RHIM) domain-mediated oligomerization, but the signaling events based on this scaffold has not been fully addressed. By using inducible dimer systems we found that RIP1âRIP1 interaction is dispensable for necroptosis; RIP1âRIP3 interaction is required for necroptosis signaling, but there is no necroptosis if no additional RIP3 protein is recruited to the RIP1âRIP3 heterodimer, and the interaction with RIP1 promotes the RIP3 to recruit other RIP3; RIP3âRIP3 interaction is required for necroptosis and RIP3âRIP3 dimerization is sufficient to induce necroptosis; and RIP3 dimer-induced necroptosis requires MLKL. We further show that RIP3 oligomer is not more potent than RIP3 dimer in triggering necroptosis, suggesting that RIP3 homo-interaction in the complex, rather than whether RIP3 has formed homo polymer, is important for necroptosis. RIP3 dimerization leads to RIP3 intramolecule autophosphorylation, which is required for the recruitment of MLKL. Interestingly, phosphorylation of one of RIP3 in the dimer is sufficient to induce necroptosis. As RIP1âRIP3 heterodimer itself cannot induce necroptosis, the RIP1âRIP3 heterodimeric amyloid fibril is unlikely to directly propagate necroptosis. We propose that the signaling events after the RIP1âRIP3 amyloid complex assembly are the recruitment of free RIP3 by the RIP3 in the amyloid scaffold followed by autophosphorylation of RIP3 and subsequent recruitment of MLKL by RIP3 to execute necroptosis.
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headline:Distinct roles of RIP1âRIP3 hetero- and RIP3âRIP3 homo-interaction in mediating necroptosis
description:Necroptosis is mediated by a signaling complex called necrosome, containing receptor-interacting protein (RIP)1, RIP3, and mixed-lineage kinase domain-like (MLKL). It is known that RIP1 and RIP3 form heterodimeric filamentous scaffold in necrosomes through their RIP homotypic interaction motif (RHIM) domain-mediated oligomerization, but the signaling events based on this scaffold has not been fully addressed. By using inducible dimer systems we found that RIP1âRIP1 interaction is dispensable for necroptosis; RIP1âRIP3 interaction is required for necroptosis signaling, but there is no necroptosis if no additional RIP3 protein is recruited to the RIP1âRIP3 heterodimer, and the interaction with RIP1 promotes the RIP3 to recruit other RIP3; RIP3âRIP3 interaction is required for necroptosis and RIP3âRIP3 dimerization is sufficient to induce necroptosis; and RIP3 dimer-induced necroptosis requires MLKL. We further show that RIP3 oligomer is not more potent than RIP3 dimer in triggering necroptosis, suggesting that RIP3 homo-interaction in the complex, rather than whether RIP3 has formed homo polymer, is important for necroptosis. RIP3 dimerization leads to RIP3 intramolecule autophosphorylation, which is required for the recruitment of MLKL. Interestingly, phosphorylation of one of RIP3 in the dimer is sufficient to induce necroptosis. As RIP1âRIP3 heterodimer itself cannot induce necroptosis, the RIP1âRIP3 heterodimeric amyloid fibril is unlikely to directly propagate necroptosis. We propose that the signaling events after the RIP1âRIP3 amyloid complex assembly are the recruitment of free RIP3 by the RIP3 in the amyloid scaffold followed by autophosphorylation of RIP3 and subsequent recruitment of MLKL by RIP3 to execute necroptosis.
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