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Titel:

Ubiquitylation of RIPK3 beyond-the-RHIM can limit RIPK3 activity and cell death.

Dokumenttyp:
Journal Article
Autor(en):
Frank, Daniel; Garnish, Sarah E; Sandow, Jarrod J; Weir, Ashley; Liu, Lin; Clayer, Elise; Meza, Lizeth; Rashidi, Maryam; Cobbold, Simon A; Scutts, Simon R; Doerflinger, Marcel; Anderton, Holly; Lawlor, Kate E; Lalaoui, Najoua; Kueh, Andrew J; Eng, Vik Ven; Ambrose, Rebecca L; Herold, Marco J; Samson, Andre L; Feltham, Rebecca; Murphy, James M; Ebert, Gregor; Pearson, Jaclyn S; Vince, James E
Abstract:
Pathogen recognition and TNF receptors signal via receptor interacting serine/threonine kinase-3 (RIPK3) to cause cell death, including MLKL-mediated necroptosis and caspase-8-dependent apoptosis. However, the post-translational control of RIPK3 is not fully understood. Using mass-spectrometry, we identified that RIPK3 is ubiquitylated on K469. The expression of mutant RIPK3 K469R demonstrated that RIPK3 ubiquitylation can limit both RIPK3-mediated apoptosis and necroptosis. The enhanced cell de...     »
Zeitschriftentitel:
iScience
Jahr:
2022
Band / Volume:
25
Heft / Issue:
7
Volltext / DOI:
doi:10.1016/j.isci.2022.104632
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/35800780
TUM Einrichtung:
Institut für Virologie (Prof. Protzer); Lehrstuhl für Molekulare Allergologie und Umweltforschung (Prof. Schmidt-Weber)
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