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

  title={p38MAPK/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection},
  author={Manoj B Menon and Julia Gropengie\sser and Jessica Fischer and L. Yu. 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},
  journal={Nature Cell Biology},
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… CONTINUE READING