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TitleStructural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9607, Year 2025
Publish dateOct 30, 2025
AuthorsPaula Polonio / Jorge Pedro López-Alonso / Hanxing Jiang / Sara Andrés-Campos / Fátima C Escobedo-González / Gustavo A Titaux-Delgado / Iban Ubarretxena-Belandia / Miguel Mompeán /
PubMed AbstractAmyloid 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 ...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.
External linksNat Commun / PubMed:41168207 / PubMed Central
MethodsEM (helical sym.)
Resolution2.57 Å
Structure data

52356

9hr6

EMDB-52356, PDB-9hr6:
cryoEM structure of amyloid fibrils formed by human RIPK1
Method: EM (helical sym.) / Resolution: 2.57 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Amyloid / kinase

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