ZBP1 mediates interferon-induced necroptosis.

Animals Caspase 8 / metabolism Cell Line Fas-Associated Death Domain Protein / metabolism Humans Interferons / pharmacology Janus Kinase 1 / metabolism Male Mice, Inbred C57BL Mice, Knockout Mutant Proteins / metabolism Necroptosis / drug effects Protein Binding / drug effects Protein Biosynthesis / drug effects Protein Domains RNA-Binding Proteins / chemistry Receptor-Interacting Protein Serine-Threonine Kinases / metabolism STAT1 Transcription Factor / metabolism Signal Transduction / drug effects Systemic Inflammatory Response Syndrome / metabolism Tumor Necrosis Factor-alpha
ZBP1 interferon necroptosis

Journal

Cellular & molecular immunology
ISSN: 2042-0226
Titre abrégé: Cell Mol Immunol
Pays: China
ID NLM: 101242872

Informations de publication

Date de publication:
04 2020
Historique:
received: 13 01 2019
accepted: 21 04 2019
pubmed: 12 5 2019
medline: 4 6 2021
entrez: 12 5 2019
Statut: ppublish

Résumé

Interferons (IFNs) play an important role in immunomodulatory and antiviral functions. IFN-induced necroptosis has been reported in cells deficient in receptor-interacting protein kinase 1 (RIPK1), Fas-associated protein with death domain (FADD), or caspase-8, but the mechanism is largely unknown. Here, we report that the DNA-dependent activator of IFN regulatory factors (ZBP1, also known as DAI) is required for both type I (β) and type II (γ) IFN-induced necroptosis. We show that L929 fibroblast cells became susceptible to IFN-induced necroptosis when RIPK1, FADD, or Caspase-8 was genetically deleted, confirming the antinecroptotic role of these proteins in IFN signaling. We found that the pronecroptotic signal from IFN stimulation depends on new protein synthesis and identified ZBP1, an IFN-stimulated gene (ISG) product, as the de novo synthesized protein that triggers necroptosis in IFN-stimulated cells. The N-terminal domain (ND) of ZBP1 is important for ZBP1-ZBP1 homointeraction, and its RHIM domain in the C-terminal region interacts with RIPK3 to initiate RIPK3-dependent necroptosis. The antinecroptotic function of RIPK1, FADD, and caspase-8 in IFN-treated cells is most likely executed by caspase-8-mediated cleavage of RIPK3, since the inhibitory effect on necroptosis was eliminated when the caspase-8 cleavage site in RIPK3 was mutated. ZBP1-mediated necroptosis in IFN-treated cells is likely physiologically relevant, as ZBP1 KO mice were significantly protected against acute systemic inflammatory response syndrome (SIRS) induced by TNF + IFN-γ.

Identifiants

DOI: 10.1038/s41423-019-0237-x PMID: 31076724 PMC: PMC7109092
pubmed: 31076724
doi: 10.1038/s41423-019-0237-x
pii: 10.1038/s41423-019-0237-x
pmc: PMC7109092
doi:

Substances chimiques

Fadd protein, mouse 0
Fas-Associated Death Domain Protein 0
Mutant Proteins 0
RNA-Binding Proteins 0
STAT1 Transcription Factor 0
Tumor Necrosis Factor-alpha 0
Zbp1 protein, mouse 0
Interferons 9008-11-1
Janus Kinase 1 EC 2.7.10.2
Receptor-Interacting Protein Serine-Threonine Kinases EC 2.7.11.1
Ripk1 protein, mouse EC 2.7.11.1
Caspase 8 EC 3.4.22.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

356-368

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Auteurs

Daowei Yang (D)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Yaoji Liang (Y)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.
Department of Cancer Prevention Diagnosis and Treatment, Cancer Hospital, The First Affiliated Hospital of Xiamen University, Teaching Hospital of Fujian Medical University, Xiamen, China.
School of Pharmaceutical Sciences, Xiamen University, Xiamen, 361102, Fujian, China.
XMU School of Pharmaceutical Sciences-Amogene Joint R&D Center for Genetic Diagnostics, Amogene Biotech, Xiamen, 361102, Fujian, China.

Shubo Zhao (S)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Yan Ding (Y)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Qiuyu Zhuang (Q)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Qilin Shi (Q)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Tingting Ai (T)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Su-Qin Wu (SQ)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China.

Jiahuai Han (J)

State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, 361005, Fujian, China. jhan@xmu.edu.cn.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › Protéines adaptatrices de signalisation des récepteurs à domaine de mort › Caspase 8 › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › Protéines adaptatrices de signalisation des récepteurs à domaine de mort › Protéine à domaine de mort associée à Fas › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Facteurs biologiques › Protéines et peptides de signalisation intercellulaire › Cytokines › Interférons › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-tyrosine kinases › Janus kinases › Janus kinase 1 › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Lignées consanguines de souris › Souris de lignée C57BL › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souris transgéniques › Souris knockout › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mutantes › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Mort cellulaire › Mort cellulaire régulée › Nécroptose › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Métabolisme › Liaison aux protéines › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Phénomènes génétiques › Expression des gènes › Biosynthèse des protéines › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Protéines de liaison à l'ARN › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Receptor-Interacting Protein Serine-Threonine Kinases › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Facteurs de transcription STAT › Facteur de transcription STAT-1 › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Transduction du signal › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Choc › Syndrome de réponse inflammatoire généralisée › ZBP1 mediates interferon-induced necroptosis.
questionsmedicales.fr › Facteurs biologiques › Protéines et peptides de signalisation intercellulaire › Cytokines › Facteurs de nécrose tumorale › Facteur de nécrose tumorale alpha › ZBP1 mediates interferon-induced necroptosis.