The phospho-barcode of RIPK1: complementarity or redundancy?

ABSTRACT

Receptor interacting serine/threonine kinase 1 (RIPK1) is the central mediator of tumor necrosis factor (TNF) signaling. It regulates both pro-survival/pro-inflammatory and cell death pathways. In order to fulfill this complex regulation, RIPK1 is regulated by several post-translational modifications, including ubiquitination, acetylation, and phosphorylation. In our recent work, we show that the unc-51-like autophagy activating kinase 1 (ULK1) phosphorylates RIPK1 at Ser357 and thus blocks TNF-induced cell death.

KEYWORDS:

• Autophagy
• necroptosis
• RIPK1
• TNF
• Ulk1

Acknowledgments

We would like to apologize to all our colleagues whose important work on RIPK1 signaling could not be cited here because of space limitations.

Disclosure of potential conflicts of interest

No potential conflicts of interest were disclosed.

Additional information

Funding

This work was supported by the Deutsche Forschungsgemeinschaft STO 864/4-1, STO 864/5-1 and GRK 2158 (to BS), and the Düsseldorf School of Oncology (to BS; funded by the Comprehensive Cancer Center Düsseldorf/Deutsche Krebshilfe and the Medical Faculty of the Heinrich Heine University Düsseldorf).