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

Author

Listed:
  • Jing Liu

    (ShanghaiTech University
    Wuhan University of Science and Technology)

  • 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
    Wuhan University of Science and Technology)

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.

Suggested Citation

  • Jing Liu & Xia-lian Wu & Jing Zhang & Bing Li & Hua-yi Wang & Jian Wang & Jun-xia Lu, 2024. "The structure of mouse RIPK1 RHIM-containing domain as a homo-amyloid and in RIPK1/RIPK3 complex," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51303-y
    DOI: 10.1038/s41467-024-51303-y
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    References listed on IDEAS

    as
    1. Myungwoon Lee & Ujjayini Ghosh & Kent R. Thurber & Masato Kato & Robert Tycko, 2020. "Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    2. Xia-lian Wu & Hong Hu & Xing-qi Dong & Jing Zhang & Jian Wang & Charles D. Schwieters & Jing Liu & Guo-xiang Wu & Bing Li & Jing-yu Lin & Hua-yi Wang & Jun-xia Lu, 2021. "The amyloid structure of mouse RIPK3 (receptor interacting protein kinase 3) in cell necroptosis," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
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