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Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1
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Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1
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Journal Article
Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1
2025
Overview
Amyloid fibrils can form biologically relevant functional assemblies. The RIP homotypic interaction motifs (RHIMs) in receptor-interacting protein kinases 1 and 3 (RIPK1 and RIPK3) orchestrate the formation of amyloid-like fibrils essential for propagating cell death signals. While the structures of human RIPK3 (hRIPK3) homomeric fibrils and RIPK1-RIPK3 heteromeric fibrils have been elucidated, the atomic structure of human RIPK1 (hRIPK1) homomeric fibrils has remained elusive. We present a high-resolution structure of hRIPK1 RHIM-mediated amyloid fibrils, determined using an integrative approach combining cryoprobe-detected solid-state nuclear magnetic resonance spectroscopy and cryo-electron microscopy. The fibrils adopt an N-shaped fold consisting of three β-sheets stabilized by hydrophobic interactions and hydrogen bonding. A key hydrogen bond between N545 and G542 closes the β2-β3 loop, resulting in denser side-chain packing compared to hRIPK3 homomeric fibrils. These findings provide structural insights into how hRIPK1 homomeric fibrils nucleate hRIPK3 recruitment and fibrillization during necroptosis, offering broader perspectives on the molecular principles governing RHIM-mediated amyloid assembly and functional amyloids.
This study reveals the atomic structure of RIPK1 fibrils, a type of physiological amyloid that helps control inflammation and regulated cell death in human cells.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/131
/ 147/143
/ 631/57
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Magnetic resonance spectroscopy
/ NMR
/ Proteins
/ Receptor-Interacting Protein Serine-Threonine Kinases - chemistry
/ Receptor-Interacting Protein Serine-Threonine Kinases - genetics
/ Receptor-Interacting Protein Serine-Threonine Kinases - metabolism
/ Receptor-Interacting Protein Serine-Threonine Kinases - ultrastructure
/ Science
/ Seeds
