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The Autophagy-Initiating Kinase ULK1 Controls RIPK1-Mediated Cell Death

Wu, Wenxian, Wang, Xiaojing, Berleth, Niklas, Deitersen, Jana, Wallot-Hieke, Nora, Böhler, Philip, Schlütermann, David, Stuhldreier, Fabian, Cox, Jan, Schmitz, Katharina, Seggewiß, Sabine, Peter, Christoph, Kasof, Gary, Stefanski, Anja, Stühler, Kai, Tschapek, Astrid, Gödecke, Axel, Stork, Björn·2020·Cell Reports
DOI 10.1016/j.celrep.2020.107547
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Abstract

Autophagy, apoptosis, and necroptosis are stress responses governing the ultimate fate of a cell. However, the crosstalk between these cellular stress responses is not entirely understood. Especially, it is not clear whether the autophagy-initiating kinase ULK1 and the cell-death-regulating kinase RIPK1 are involved in this potential crosstalk. Here, we identify RIPK1 as a substrate of ULK1. ULK1-dependent phosphorylation of RIPK1 reduces complex IIb/necrosome assembly and tumor necrosis factor (TNF)-induced cell death, whereas deprivation of ULK1 enhances TNF-induced cell death. We observe that ULK1 phosphorylates multiple sites of RIPK1, but it appears that especially phosphorylation of S357 within the intermediate domain of RIPK1 mediates this cell-death-inhibiting effect. We propose that ULK1 is a regulator of RIPK1-mediated cell death.

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Metadata

Authors
Wu, W., Wang, X., Berleth, N., Deitersen, J., Wallot-Hieke, N., Böhler, P., Schlütermann, D., Stuhldreier, F., Cox, J., Schmitz, K., Seggewiß, S., Peter, C., Kasof, G., Stefanski, A., Stühler, K., Tschapek, A., Gödecke, A., & Stork, B.
Venue
Cell Reports
Publisher
Elsevier BV
Published
2020-04
Volume
31
Issue
3
Pages
107547
ISSN
2211-1247
DOI
10.1016/j.celrep.2020.107547
Cited by
72
References
10
Language
en
Licence
Funders
Deutsche Forschungsgemeinschaft

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