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TitleElectric dipole moment drives the dynamics of the TNFR1 complex I signalosome.
Journal, issue, pagesNature, Vol. 653, Issue 8116, Page 1196-1204, Year 2026
Publish dateApr 1, 2026
AuthorsJianping Liu / Jing Zhao / Jiayang Gao / Kun Zhao / Yaoyao Han / Jing Yang / Zefei Li / Jianyu Ye / Ziyu Sun / Fengyi Wang / Xinyi Liu / Zekai Li / Siyu Ji / Bo Liu / Cong Liu / Yixiao Zhang / Junying Yuan / James J Chou /
PubMed AbstractDynamic assembly of the complex I signalosome mediated by three death domain (DD)-containing proteins-TNFR1, TRADD and RIPK1-is key for transmitting extracellular TNF stimuli to intracellular NF-κB ...Dynamic assembly of the complex I signalosome mediated by three death domain (DD)-containing proteins-TNFR1, TRADD and RIPK1-is key for transmitting extracellular TNF stimuli to intracellular NF-κB signalling in controlling 'live or die' cell fate. This signalling hub features the rapid recruitment of TRADD and RIPK1 after engagement of TNFR1 by TNF for the formation of complex I, followed by timed disassembly for transition into downstream signalling complexes, but the mechanism driving the dynamic reversibility of complex I remains unclear. Here we captured the assembly core of complex I and determined its cryo-electron microscopy structure, showing a pentameric fibre comprising 31 DDs, with a single layer of a TRADD-DD pentamer sandwiched between multiple layers of TNFR1-DD and RIPK1-DD homopentamers. Structural analysis revealed a strong opposing electric dipole moment (EDM) generated by RIPK1-DD oligomerization relative to that of TNFR1-DD and TRADD-DD. Structure-guided mutagenesis in TNFR1-TRADD-RIPK1 pentameric fibres altering the EDM without affecting DD oligomerization demonstrated the role and mechanism of EDM in driving the dynamic reversibility mediating the rapid assembly and disassembly of complex I. Our study demonstrates a role for long-range interactions mediated by protein EDMs in driving the assembly and disassembly of super-signalling complex I for promoting NF-κB signalling.
External linksNature / PubMed:41922760
MethodsEM (helical sym.) / EM (single particle)
Resolution2.62 - 3.41 Å
Structure data

64869

9v9c

EMDB-64869, PDB-9v9c:
Cryo-EM structure of human TNFR1 DD filament
Method: EM (helical sym.) / Resolution: 2.62 Å

64870

9v9e

EMDB-64870, PDB-9v9e:
Cryo-EM structure of human RIPK1 DD filament
Method: EM (helical sym.) / Resolution: 2.87 Å

65047

9vgd

EMDB-65047, PDB-9vgd:
Helical assembly of TRADD death domain
Method: EM (helical sym.) / Resolution: 3.3 Å

65094

9vin

EMDB-65094, PDB-9vin:
Ternary complex of TNFR1-DD, TRADD-DD and RIPK1-DD
Method: EM (single particle) / Resolution: 3.41 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Death doamin / APOPTOSIS / Death domain / Inflammation / Tumor necrosis factor / TNFR1 / RIPK1 / TRADD

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