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RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition
Open accessAbstract
Significance: The protein kinase receptor interacting protein 1 controls signaling via death receptors, Toll-like receptors, and retinoic acid-inducible gene 1-like receptors, dictating inflammatory outcomes as broad as cytokine activation and cell death. RIP1 makes a vital contribution during development, evident from the fact that RIP1-deficient mice die soon after birth. Here, we show that a kinase-independent function of RIP1 dampens the consequences of innate immune cell death. During parturition, RIP1 prevents the lethal consequences of RIP3-dependent necroptosis as well as caspase 8 (Casp8)-dependent apoptosis. In contrast to the RIP1-deficient phenotype, mice lacking a combination of RIP1, RIP3, and Casp8 are born and mature into viable, fertile, and immunocompetent adults. These results demonstrate the important protective role of RIP1 against physiologic and microbial death cues encountered at birth.
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“Moreover, Ripk1−/− cells display increased sensitivity to necroptosis and/or extrinsic apoptosis induced by a set of innate immune stimuli [499].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [499]
In the citing paper
“Intriguingly, the pro-survival role of RIPK1 in development seems to be independent of both its kinase activity and RIPK3 binding, as demonstrated by the fact that mice genetically engineered to express a kinase-dead variant of RIPK1 (e.g., RIPK1K45A) are viable and fertile [447, 499, 508].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [499]
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“…have constructed Rip1-/-Rip3-/-Casp8-/- or Rip1-/-Rip3-/-Fadd-/- mice, which behave normally after birth in contrast to Rip1-/- mice, suggesting the postnatal lethality of Rip1-/- mice is induced by the synergy of caspase-8 and RIP3 (Dillon et al., 2014; Kaiser et al., 2014; Rickard et al., 2014).”
BackgroundSchäffer, A. A. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733657254.793550650
Cell death: RIPK1 protects epithelial cells
Baumann, K. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3900
Tan, Y., Sementino, E., Cheung, M., Peri, S., Menges, C. W., Kukuyan, A.-M., Zhang, T., Khazak, V., Fox, L. A., Ross, E. A., et al. (2023) · doi:10.1158/1078-0432.c.6528651.v1
Self-citationNovel functions of LUBAC-mediated M1 poly-ubiquitination in TNFR1-mediated necroptosis
Weinelt, N. (2024) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.81732
Cell Death Mechanisms, Associated Toxicity and Therapeutic Applications
Davila, J. C., Kovalova, N., & Radi, Z. A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00265-5
Cell Death Regulates Injury and Inflammation During Renal Allograft Transplantation
Lau, A. N. (2014) · Scholarship@Western (Western University)
Targeting PANoptosis in atherosclerosis: bridging cell death mechanisms and therapy
Hu, L., Sun, C., Xiaoya, L. I., ZHANG, X., Zongliang, Y. U., Liang, L. I., Min, W. U., & Longtao, L. I. U. (2026) · APOPTOSIS · doi:10.1007/s10495-025-02230-w
“RIPK1⁻/⁻ cells, for example, are highly sensitive to TNF-induced apoptosis, whereas RIPK1⁻/⁻Casp8⁻/⁻ cells undergo RIPK3-MLKL–dependent necroptosis [48 ].”
Caractérisation de nouveaux inhibiteurs de la kinase RIPK1 et de la nécroptose
Cann, F. L. (2017) · theses.fr (ABES) · doi:10.70675/14750b73za612z432ezbf7cz5b72ea09e2e5
RIPK1 ubiquitination regulates its kinase-independent function in development and inflammation
Li, M., Liu, J., Xing, M., Liu, H., Wang, L., Wu, X., Ou, Y., Zhao, X., Wang, Y., Xie, Y., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2520356123
“…the inflammatory phenotypes observed in RIPK1 K376R/D138N double - mutant mice closely resem ble those seen in RIPK1 - deficient backgrounds (6–8), indicating that dysregulation of the RIPK1 scaffold - rather than its complete loss - can similarly trigger IL - 1 β –driven systemic…”
Sawant, P., Wolf, H., Mathew, A., Bensalel, J., Gallego‐Delgado, J., & Mandal, P. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1759368
“RIPK1 associates with both CASP8 and RIPK3 to aid in extrinsic apoptosis or necroptosis (61, 65, 80).”
Self-citationThe dual role of RIPK family in IBD: from cell death to therapeutic targeting
Jiang, L., Gou, A., Kang, A., Yan, F., Qiao, Y., Xu, F., & Bai, Y. (2026) · Molecular Medicine · doi:10.1186/s10020-026-01556-8
“However, the lethality is fully rescued by concomitant deletion of Casp8 and Ripk3 , as triple-knockout mice lacking all three genes develop into viable and fertile adults with normal hematopoiesis (Dillon et al. 2014; Rickard et al. 2014; Kaiser et al. 2014).”
PANoptosis in the pathogenesis of myelodysplastic syndromes
Thalla, R., Lamichhane, J., Lewis, C., Breslin, P., & Zhang, J. (2026) · Molecular Oncology · doi:10.1002/1878-0261.70309
The anti-tumour activity of TNF in melanoma is determined by cFLIP
Stachelscheid, J., Kaul, C., Gerstenberg, K., Werthenbach, J. P., Schorn, F., Steinkamp, J., Zigrino, P., Pasparakis, M., Schiffmann, L. M., & Kashkar, H. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-09154-6
Z-Nucleic Acid-Binding Protein (ZBP)1 (DAI/DLM1) Regulation in Antiviral Cell Death Pathways
Mocarski, E. S., & Guo, H. (2026) · Pathogens · doi:10.3390/pathogens15090972
“…of fertile and otherwise immunocompetent mice that retain sufficient innate and adaptive immune competence to be able to control viral infection [51,61] and (2) the stage was set to dissect the distinct contributions of both CASP8-and RIPK3-regulated signaling pathways to host defense and…”
Self-citationBindingDB Entry 50022494: RIP3 induces apoptosis independent of pronecrotic kinase activity.
BindingDB (2025) · UC San Diego · doi:10.7270/q2b2810v
BindingDB Entry 50019664: From (Tool)Bench to Bedside: The Potential of Necroptosis Inhibitors.
BindingDB (2024) · UC San Diego · doi:10.7270/q2x92gpm
Metadata
- Authors
- Kaiser, W. J., Daley-Bauer, L. P., Thapa, R. J., Mandal, P., Berger, S. B., Huang, C., Sundararajan, A., Guo, H., Roback, L., Speck, S. H., Bertin, J., Gough, P. J., Balachandran, S., & Mocarski, E. S.
- Affiliations
- Emory University (US)
- Department of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA 30322;
- Fox Chase Cancer Center (US)
- GlaxoSmithKline (United States) (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-05-12
- Volume
- 111
- Issue
- 21
- Pages
- 7753-7758
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4040608
- OpenAlex
- W2069250210
- Cited by
- 291
- References
- 41
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 17 · 2023: 14 · 2022: 17 · 2021: 24 · 2020: 28 · 2019: 29 · 2018: 25 · 2017: 26 · 2016: 39 · 2015: 30 · 2014: 22
- FWCI
- 15.90
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (DP5OD012198)
- U.S. Public Health Service (R5630363)
- National Cancer Institute (R01CA168621, T32CA009035)
- National Institute of Allergy and Infectious Diseases (R01AI020211, R21AI104212, R01AI118853)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- RIPK1, RIPK3, caspase-8, necroptosis, apoptosis, innate immunity, childbirth, perinatal lethality, kinase-independent function, TNF-α, interferon, double-stranded RNA, antiviral immunity
- MeSH terms
- Animals, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Immunity, Innate, Necrosis, Immunoblotting, Signal Transduction, Apoptosis, DNA Primers, Mice, Knockout, GTPase-Activating Proteins, Parturition, Mice, Caspase 8, Receptor-Interacting Protein Serine-Threonine Kinases, Gene Knock-In Techniques
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