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p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection

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p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection. / Menon, Manoj B; Gropengießer, Julia; Fischer, Jessica; Novikova, Lena; Deuretzbacher, Anne; Lafera, Juri; Schimmeck, Hanna; Czymmeck, Nicole; Ronkina, Natalia; Kotlyarov, Alexey; Aepfelbacher, Martin; Gaestel, Matthias; Ruckdeschel, Klaus.

in: NAT CELL BIOL, Jahrgang 19, Nr. 10, 10.2017, S. 1248-1259.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Menon, MB, Gropengießer, J, Fischer, J, Novikova, L, Deuretzbacher, A, Lafera, J, Schimmeck, H, Czymmeck, N, Ronkina, N, Kotlyarov, A, Aepfelbacher, M, Gaestel, M & Ruckdeschel, K 2017, 'p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection', NAT CELL BIOL, Jg. 19, Nr. 10, S. 1248-1259. https://doi.org/10.1038/ncb3614

APA

Menon, M. B., Gropengießer, J., Fischer, J., Novikova, L., Deuretzbacher, A., Lafera, J., Schimmeck, H., Czymmeck, N., Ronkina, N., Kotlyarov, A., Aepfelbacher, M., Gaestel, M., & Ruckdeschel, K. (2017). p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection. NAT CELL BIOL, 19(10), 1248-1259. https://doi.org/10.1038/ncb3614

Vancouver

Menon MB, Gropengießer J, Fischer J, Novikova L, Deuretzbacher A, Lafera J et al. p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection. NAT CELL BIOL. 2017 Okt;19(10):1248-1259. https://doi.org/10.1038/ncb3614

Bibtex

@article{bf47a536f7334b5e903c0b718a434364,
title = "p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection",
abstract = "Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by phosphoproteomic screens using LPS-treated macrophages and stress-stimulated embryonic fibroblasts. p38MAPK/MK2 interact with RIPK1 in a cytoplasmic complex and MK2 phosphorylates mouse RIPK1 at Ser321/336 in response to pro-inflammatory stimuli, such as TNF and LPS, and infection with the pathogen Yersinia enterocolitica. MK2 phosphorylation inhibits RIPK1 autophosphorylation, curtails RIPK1 integration into cytoplasmic cytotoxic complexes, and suppresses RIPK1-dependent apoptosis and necroptosis. In Yersinia-infected macrophages, RIPK1 phosphorylation by MK2 protects against infection-induced apoptosis, a process targeted by Yersinia outer protein P (YopP). YopP suppresses p38MAPK/MK2 activation to increase Yersinia-driven apoptosis. Hence, MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.",
keywords = "Animals, Apoptosis, Bacterial Proteins, Cytosol, Female, Genotype, HEK293 Cells, Host-Pathogen Interactions, Humans, I-kappa B Kinase, Inflammation, Intracellular Signaling Peptides and Proteins, MAP Kinase Kinase Kinases, Macrophages, Male, Membrane Proteins, Mice, Knockout, Necrosis, Phenotype, Phosphorylation, Protein-Serine-Threonine Kinases, Receptor-Interacting Protein Serine-Threonine Kinases, Receptors, Tumor Necrosis Factor, Type I, Serine, Signal Transduction, Time Factors, Transfection, Tumor Necrosis Factor-alpha, Yersinia Infections, Yersinia enterocolitica, p38 Mitogen-Activated Protein Kinases, Journal Article",
author = "Menon, {Manoj B} and Julia Gropengie{\ss}er and Jessica Fischer and Lena Novikova and Anne Deuretzbacher and Juri Lafera and Hanna Schimmeck and Nicole Czymmeck and Natalia Ronkina and Alexey Kotlyarov and Martin Aepfelbacher and Matthias Gaestel and Klaus Ruckdeschel",
year = "2017",
month = oct,
doi = "10.1038/ncb3614",
language = "English",
volume = "19",
pages = "1248--1259",
journal = "NAT CELL BIOL",
issn = "1465-7392",
publisher = "NATURE PUBLISHING GROUP",
number = "10",

}

RIS

TY - JOUR

T1 - p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection

AU - Menon, Manoj B

AU - Gropengießer, Julia

AU - Fischer, Jessica

AU - Novikova, Lena

AU - Deuretzbacher, Anne

AU - Lafera, Juri

AU - Schimmeck, Hanna

AU - Czymmeck, Nicole

AU - Ronkina, Natalia

AU - Kotlyarov, Alexey

AU - Aepfelbacher, Martin

AU - Gaestel, Matthias

AU - Ruckdeschel, Klaus

PY - 2017/10

Y1 - 2017/10

N2 - Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by phosphoproteomic screens using LPS-treated macrophages and stress-stimulated embryonic fibroblasts. p38MAPK/MK2 interact with RIPK1 in a cytoplasmic complex and MK2 phosphorylates mouse RIPK1 at Ser321/336 in response to pro-inflammatory stimuli, such as TNF and LPS, and infection with the pathogen Yersinia enterocolitica. MK2 phosphorylation inhibits RIPK1 autophosphorylation, curtails RIPK1 integration into cytoplasmic cytotoxic complexes, and suppresses RIPK1-dependent apoptosis and necroptosis. In Yersinia-infected macrophages, RIPK1 phosphorylation by MK2 protects against infection-induced apoptosis, a process targeted by Yersinia outer protein P (YopP). YopP suppresses p38MAPK/MK2 activation to increase Yersinia-driven apoptosis. Hence, MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.

AB - Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by phosphoproteomic screens using LPS-treated macrophages and stress-stimulated embryonic fibroblasts. p38MAPK/MK2 interact with RIPK1 in a cytoplasmic complex and MK2 phosphorylates mouse RIPK1 at Ser321/336 in response to pro-inflammatory stimuli, such as TNF and LPS, and infection with the pathogen Yersinia enterocolitica. MK2 phosphorylation inhibits RIPK1 autophosphorylation, curtails RIPK1 integration into cytoplasmic cytotoxic complexes, and suppresses RIPK1-dependent apoptosis and necroptosis. In Yersinia-infected macrophages, RIPK1 phosphorylation by MK2 protects against infection-induced apoptosis, a process targeted by Yersinia outer protein P (YopP). YopP suppresses p38MAPK/MK2 activation to increase Yersinia-driven apoptosis. Hence, MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.

KW - Animals

KW - Apoptosis

KW - Bacterial Proteins

KW - Cytosol

KW - Female

KW - Genotype

KW - HEK293 Cells

KW - Host-Pathogen Interactions

KW - Humans

KW - I-kappa B Kinase

KW - Inflammation

KW - Intracellular Signaling Peptides and Proteins

KW - MAP Kinase Kinase Kinases

KW - Macrophages

KW - Male

KW - Membrane Proteins

KW - Mice, Knockout

KW - Necrosis

KW - Phenotype

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - Receptor-Interacting Protein Serine-Threonine Kinases

KW - Receptors, Tumor Necrosis Factor, Type I

KW - Serine

KW - Signal Transduction

KW - Time Factors

KW - Transfection

KW - Tumor Necrosis Factor-alpha

KW - Yersinia Infections

KW - Yersinia enterocolitica

KW - p38 Mitogen-Activated Protein Kinases

KW - Journal Article

U2 - 10.1038/ncb3614

DO - 10.1038/ncb3614

M3 - SCORING: Journal article

C2 - 28920954

VL - 19

SP - 1248

EP - 1259

JO - NAT CELL BIOL

JF - NAT CELL BIOL

SN - 1465-7392

IS - 10

ER -