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RIPK1 inhibits ZBP1-driven necroptosis during development
Abstract
Receptor-interacting protein kinase 1 (RIPK1) promotes cell survival-mice lacking RIPK1 die perinatally, exhibiting aberrant caspase-8-dependent apoptosis and mixed lineage kinase-like (MLKL)-dependent necroptosis. However, mice expressing catalytically inactive RIPK1 are viable, and an ill-defined pro-survival function for the RIPK1 scaffold has therefore been proposed. Here we show that the RIP homotypic interaction motif (RHIM) in RIPK1 prevents the RHIM-containing adaptor protein ZBP1 (Z-DNA binding protein 1; also known as DAI or DLM1) from activating RIPK3 upstream of MLKL. Ripk1 RHIM/RHIM mice that expressed mutant RIPK1 with critical RHIM residues IQIG mutated to AAAA died around birth and exhibited RIPK3 autophosphorylation on Thr231 and Ser232, which is a hallmark of necroptosis, in the skin and thymus. Blocking necroptosis with catalytically inactive RIPK3(D161N), RHIM mutant RIPK3, RIPK3 deficiency, or MLKL deficiency prevented lethality in Ripk1 RHIM/RHIM mice. Loss of ZBP1, which engages RIPK3 in response to certain viruses but previously had no defined role in development, also prevented perinatal lethality in Ripk1 RHIM/RHIM mice. Consistent with the RHIM of RIPK1 functioning as a brake that prevents ZBP1 from engaging the RIPK3 RHIM, ZBP1 interacted with RIPK3 in Ripk1 RHIM/RHIM Mlkl-/- macrophages, but not in wild-type, Mlkl-/- or Ripk1 RHIM/RHIM Ripk3 RHIM/RHIM macrophages. Collectively, these findings indicate that the RHIM of RIPK1 is critical for preventing ZBP1/RIPK3/MLKL-dependent necroptosis during development.
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“or (2) ZBP1, which operates as a sensor for cytosolic DNA-promoting type I interferon (IFN) synthesis and NF-κB activation [439–441].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [441]
In the citing paper
“Moreover, mice expressing a variant of RIPK1 mutated in the RHIM domain die perinatally, a phenotype that can be rescued by concurrent Ripk3, Mlkl, or Zbp1 (but not Ticam1) deletion, as well as by the knock-in of catalytically inactive RIPK3 or RIPK3 mutated in the RHIM domain [440, 441].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [441]
In the citing paper
“ZBP1 acts at the initial steps of necroptosis by mediating the sequential activation of RIPK3 and MLKL.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [441]
Citations
Cites
Role of Adaptor TRIF in the MyD88-Independent Toll-Like Receptor Signaling Pathway
Yamamoto, M., Sato, S., Hemmi, H., Hoshino, K., Kaisho, T., Sanjo, H., Takeuchi, O., Sugiyama, M., Okabe, M., Takeda, K., et al. (2003) · Science · doi:10.1126/science.1087262 · Cited by 3,286
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931
DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
Takaoka, A., Wang, Z., Choi, M. K., Yanai, H., Negishi, H., Ban, T., Lu, Y., Miyagishi, M., Kodama, T., Honda, K., et al. (2007) · Nature · doi:10.1038/nature06013 · Cited by 1,704
The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism
Murphy, J. M., Czabotar, P. E., Hildebrand, J. M., Lucet, I. S., Zhang, J.-G., Alvarez-Diaz, S., Lewis, R., Lalaoui, N., Metcalf, D., Webb, A. I., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.018 · Cited by 1,220
Self-citationIAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218
Self-citationBertrand, M. J. M., Milutinovic, S., Dickson, K. M., Ho, W. C., Boudreault, A., Durkin, J. P., Gillard, J. W., Jaquith, J. B., Morris, S. J., & Barker, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.014 · Cited by 1,132
The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal
Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102
Ea, C.-K., Deng, L., Xia, Z.-P., Pineda, G., & Chen, Z. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.026 · Cited by 1,026
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Nucleic acid-protein condensates in innate immunity
Loucas, G., Locker, N., & Parker, R. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.014 · Cited by 7
Xia, Y., Li, M., Chen, Z., Fan, M., Pan, Q., Tian, Y., Liu, X., Du, P., & Li, J. (2025) · Cells · doi:10.3390/cells14231878 · Cited by 6
The kinase domain of RIPK3 tunes its scaffolding functions
Chiou, S., Horne, C. R., Patel, K. M., Preaudet, A., Rickard, J. A., Young, S. N., Jois, A., Garnish, S. E., Hempel, A., Hall, C. M., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01677-x · Cited by 6
Zhang, H., Wu, X., Li, M., Li, X., Wang, L., Liu, J., Ou, Y., Wu, X., Xing, M., Li, F., et al. (2022) · ImmunoHorizons · doi:10.4049/immunohorizons.2200021 · Cited by 7
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Herbert, A. G. (2024) · Genes and Immunity · doi:10.1038/s41435-024-00277-4 · Cited by 6
Zhou, H., Zhou, M., Liao, X., Zhang, L., Wei, H., Lu, Y., Zhang, Y., Huang, H., Hu, Y., Chen, T., et al. (2025) · Advanced Science · doi:10.1002/advs.202413675 · Cited by 6
Soe, Y. M., Sim, S.-L., & Kumari, S. (2025) · Viruses · doi:10.3390/v17020241 · Cited by 7
Williams, E. P., Xue, Y., Vogel, P., Yang, D., Flores, A. B., Li, X., Ogorek, T. J., Saini, M., Iulek, J., Ruiz, F. X., et al. (2025) · Journal of Virology · doi:10.1128/jvi.01679-24 · Cited by 6
Gelles, J. D., Mohammed, J. N., Santos, L. C., Legarda, D., Ting, A. T., & Chipuk, J. E. (2020) · STAR Protocols · doi:10.1016/j.xpro.2020.100034 · Cited by 5
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The role of ZBP1 in eccentric exercise-induced skeletal muscle necroptosis
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Mocarski, E. S., & Mandal, P. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001371 · Cited by 5
Yeap, H. W., Goh, G. R., Rosli, S. N., Pung, H. S., Giogha, C., Eng, V. V., Pearson, J. S., Hartland, E. L., & Chen, K. W. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00412-5 · Cited by 6
Guo, Z., Zhong, S.-J., Bai, J.-P., Lang, X.-Y., Cao, M., Hu, Y., Qin, X., & Sun, Y. (2025) · Scientific Reports · doi:10.1038/s41598-025-05994-y · Cited by 4
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Patton, T., Sarani, H., Somuncuoglu, N., Lawlor, K. E., & Corbett, A. J. (2025) · Trends in Immunology · doi:10.1016/j.it.2025.10.015 · Cited by 4
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Zhang, J., Tu, H., Zheng, Z., Zhao, X., & Lin, X. (2023) · Oncogene · doi:10.1038/s41388-023-02669-8 · Cited by 5
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MAGO, E., Xu, J., Weng, D., & Pan, Y. (2025) · Biocell · doi:10.32604/biocell.2025.059432 · Cited by 3
Wang, S. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1618438 · Cited by 2
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Priem, D., Dondelinger, Y., & Bertrand, M. J. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8754-2_17 · Cited by 4
Dixit, V. M. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0294-9 · Cited by 3
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Fu, Y., Yang, Y., Li, Q., Xia, X., Peng, M., Meng, S., Shen, R., Zhu, Y., Jiao, H., KIM, C. S., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110856 · Cited by 2
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Williams, E. P., Xue, Y., Yang, D., Lee, J., Kim, E., Flores, A. B., Zalduondo, L., Cao, X., Chung, D., Golden, J. E., et al. (2025) · Antiviral Research · doi:10.1016/j.antiviral.2025.106206 · Cited by 2
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Liang, Z., Taylor, S., Goradia, A., Heraud-Farlow, J. E., & Walkley, C. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.24.497437 · Cited by 2
Xu, F., Li, X., Wu, R., Qi, H., Jin, J., Liu, Z., Wu, Y., Lin, H., Shen, C., & Shuai, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.23.525173 · Cited by 2
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Yang, Y., Wang, Y., Wang, Y., Wu, E., Chen, H., Sun, L., Zhang, C., Cao, S., LI, J., Qiang, H., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.26.640344 · Cited by 2
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Kong, X., Yang, Y., Li, H., Cui, W., Wu, X., Gong, M., & Li, Y. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10202-2 · Cited by 1
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Zhang, H., Li, M., Liu, Y., Xu, C., Zhao, Q., Liu, J., Xing, M., Li, X., Zhang, H.-W., Wu, X., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-712049/v1 · Cited by 1
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Wang, L., Zhang, X., Zhang, H., Lu, K., Li, M., Li, X., Ou, Y., Zhao, X., Wu, X., Wu, X., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.24.529806 · Cited by 1
Sun, N. D., Carr, A. R., Krogman, E. N., Chawla, Y., Zhong, J., Guttormson, M. C., Chan, M., Hsu, M. A., Dong, H., Bogunovic, D., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606693 · Cited by 1
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Lü, H., Jiang, J., Huang, X., Haig, A. R., Gunaratman, L., Jevnikar, A. M., & Zhang, Z. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.05.611429 · Cited by 1
Pham, C. L. L., Strange, M., Carroll, A. O., Shanmugam, N., Sierecki, E., Gambin, Y., Steain, M. C., & Sunde, M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/324590
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Roedig, J. (2021) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.60925
Silke, J. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727819615.793545682
Luo, X. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732907680.793549325
Viegas, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219482119
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Mamoor, S. (2023) · OSF Preprints (OSF Preprints) · doi:10.31219/osf.io/r8xw4
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Metadata
- Authors
- Newton, K., Wickliffe, K. E., Maltzman, A., Dugger, D. L., Strasser, A., Pham, V. C., Lill, J. R., Roose-Girma, M., Warming, S., Solon, M., Ngu, H., Webster, J. D., & Dixit, V. M.
- Affiliations
- Genentech (US)
- The University of Melbourne (AU)
- Corresponding author
- Newton, Kim
- Dixit, Vishva M.
- ORCID
- Venue
- Nature
- Published
- 2016-11-07
- Volume
- 540
- Issue
- 7631
- Pages
- 129-133
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2547118804
- Cited by
- 390
- References
- 32
- Citations by year
- 2026: 29 · 2025: 47 · 2024: 42 · 2023: 37 · 2022: 42 · 2021: 49 · 2020: 52 · 2019: 36 · 2018: 38 · 2017: 17 · 2016: 1
- FWCI
- 15.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Genentech
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- RIPK1, ZBP1, necroptosis, RIPK3, MLKL, RHIM domain, perinatal lethality, developmental cell death, innate immunity, thymus, DAI
- MeSH terms
- Animals, Animals, Newborn, Embryo, Mammalian, Female, Glycoproteins, Macrophages, Male, Mutation, Necrosis, Phosphorylation, Protein Binding, Protein Kinases, Tumor Necrosis Factor-alpha, RNA-Binding Proteins, Apoptosis, Amino Acid Motifs, Adaptor Proteins, Vesicular Transport, Mice, Caspase 8, Receptor-Interacting Protein Serine-Threonine Kinases
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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