Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation-Reference-Cited by-同舟云学术

Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation

Published:2019-04-15 Issue:1 Volume:10 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Dondelinger Yves,Delanghe Tom,Priem Dario,Wynosky-Dolfi Meghan A.^ORCID,Sorobetea Daniel,Rojas-Rivera Diego,Giansanti Piero,Roelandt Ria,Gropengiesser Julia,Ruckdeschel Klaus^ORCID,Savvides Savvas N.^ORCID,Heck Albert J. R.^ORCID,Vandenabeele Peter^ORCID,Brodsky Igor E.^ORCID,Bertrand Mathieu J. M.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-019-09690-0.pdf

Reference63 articles.

1. Silke, J., Rickard, J. A. & Gerlic, M. The diverse role of RIP kinases in necroptosis and inflammation. Nat. Immunol. 16, 689–697 (2015).

2. Kelliher, M. A. et al. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 8, 297–303 (1998).

3. Berger, S. B. et al. Cutting Edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. J. Immunol. 192, 5476–5480 (2014).

4. Polykratis, A. et al. Cutting edge: RIPK1 Kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo. J. Immunol. 193, 1539–1543 (2014).

5. Pearson, J. S. et al. EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation. Nat Microbiol 2, 16258 (2017).

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