PuSH - Publikationsserver des Helmholtz Zentrums München: Ubiquitylation of RIPK3 beyond-the-RHIM can limit RIPK3 activity and cell death.

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Frank, D.* ; Garnish, S.E.* ; Sandow, J.J.* ; Weir, A.* ; Liu, L.* ; Clayer, E. ; Meza, L.* ; Rashidi, M.* ; Cobbold, S.A.* ; Scutts, S.R.* ; Doerflinger, M.* ; Anderton, H.* ; Lawlor, K.E.* ; Lalaoui, N.* ; Kueh, A.J.* ; Eng, V.V.* ; Ambrose, R.L.* ; Herold, M.J.* ; Samson, A.L.* ; Feltham, R.* ; Murphy, J.M.* ; Ebert, G. ; Pearson, J.S.* ; Vince, J.E.*

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

iScience 25:104632 (2022)

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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. Ripk3K469R/K469R mice challenged with Salmonella displayed enhanced bacterial loads and reduced serum IFNγ. However, Ripk3K469R/K469R macrophages and dermal fibroblasts were not sensitized to RIPK3-mediated apoptotic or necroptotic signaling suggesting that, in these cells, there is functional redundancy with alternate RIPK3 ubiquitin-modified sites. Consistent with this idea, the mutation of other ubiquitylated RIPK3 residues also increased RIPK3 hyper-ubiquitylation and cell death. Therefore, the targeted ubiquitylation of RIPK3 may act as either a brake or accelerator of RIPK3-dependent killing.

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