The structure of mouse RIPK1 RHIM-containing domain as a homo-amyloid and in RIPK1/RIPK3 complex

Jing Liu, Xia-lian Wu, Jing Zhang, Bing Li, Hua-yi Wang, Jian Wang () and Jun-xia Lu ()
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Jing Liu: ShanghaiTech University
Xia-lian Wu: Wuhan University of Science and Technology
Jing Zhang: ShanghaiTech University
Bing Li: ShanghaiTech University
Hua-yi Wang: Ltd.
Jian Wang: ShanghaiTech University
Jun-xia Lu: ShanghaiTech University

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract Receptor-interacting protein kinase 1 (RIPK1) is a therapeutic target in treating neurodegenerative diseases and cancers. RIPK1 has three distinct functional domains, with the center domain containing a receptor-interacting protein homotypic interaction motif (RHIM), which mediates amyloid formation. The functional amyloid formed by RIPK1 and/or RIPK3 is a crucial intermediate in regulating cell necroptosis. In this study, the amyloid structure of mouse RIPK1, formed by an 82-residue sequence centered at RHIM, is presented. It reveals the “N”-shaped folding of the protein subunit in the fibril with four β-strands. The folding pattern is shared by several amyloid structures formed by proteins with RHIM, with the central β-strand formed by the most conserved tetrad sequence I/VQI/VG. However, the solid-state NMR results indicate a structural difference between mouse RIPK1 and mouse RIPK3. A change in the structural rigidity is also suggested by the observation of weakened signals for mouse RIPK3 upon mixing with RIPK1 to form the RIPK1/RIPK3 complex fibrils. Our results provide vital information to understand the interactions between different proteins with RHIM, which will help us further comprehend the regulation mechanism in cell necroptosis.

Date: 2024
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DOI: 10.1038/s41467-024-51303-y

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