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Article

p38MAPK/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection.

Nature cell biology - 1 Oct 2017

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

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 28920954
DOI: 10.1038/ncb3614

Genes

RIPK1
TNF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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