Ubiquitylation of RIPK3 beyond-the-RHIM can limit RIPK3 activity and cell death.
Cell biology
Molecular biology
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
15 Jul 2022
15 Jul 2022
Historique:
received:
04
08
2021
revised:
31
03
2022
accepted:
13
06
2022
entrez:
8
7
2022
pubmed:
9
7
2022
medline:
9
7
2022
Statut:
epublish
Résumé
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 death of overexpressed RIPK3 K469R and activated endogenous RIPK3 correlated with an overall increase in RIPK3 ubiquitylation.
Identifiants
pubmed: 35800780
doi: 10.1016/j.isci.2022.104632
pii: S2589-0042(22)00904-X
pmc: PMC9254354
doi:
Types de publication
Journal Article
Langues
eng
Pagination
104632Informations de copyright
© 2022 The Authors.
Déclaration de conflit d'intérêts
J.M.M. and A.L.S. contribute to a project developing necroptosis inhibitors in collaboration with Anaxis Pharma.
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