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Structural dynamics and pH-regulated membrane binding of the TRAF2-NC trimer.
Protein Sci. 35:e70817 (2026)
Tumor necrosis factor receptor-associated factor 2 (TRAF2) is a key adaptor in TNF receptor-signaling that operates as a trimeric assembly. Here we investigate the structural and functional properties of a TRAF2 construct spanning the trimerization and receptor-binding domains (TRAF2-NC, residues 266-501). According to SAXS data, under physiological conditions, TRAF2-NC preserves a stable trimeric structure with signs of conformational flexibility. Conversely, in a mildly acidic environment (pH 5.7), the protein adopts a less compact and more heterogeneous conformation. In this condition, fluorescence energy transfer measurements reveal an increased membrane-binding propensity in the presence of ganglioside GM1. Together, these results indicate that TRAF2 oligomerization is modulated by pH-dependent conformational changes, suggesting that increased structural flexibility and partial exposure of hydrophobic regions facilitate membrane association under stress conditions, and providing a mechanistic link between structural dynamics and TRAF2 function.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Tnf Receptor Signaling ; Traf2 ; Lipid Interaction ; Membrane Binding ; Structural Dynamics ; Trimerization; Small-angle Scattering; X-ray-scattering; Lipid Rafts; Traf2; Recognition; Modulation; Gromacs; Protein; Domain
ISSN (print) / ISBN
0961-8368
e-ISSN
1469-896X
Journal
Protein Science
Quellenangaben
Volume: 35,
Issue: 11,
Article Number: e70817
Publisher
Wiley
Publishing Place
111 River St, Hoboken 07030-5774, Nj Usa
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Fondazione AIRC per la ricerca sul cancro ETS
Ministero dell'Universit e della Ricerca
Ministero dell'Universit e della Ricerca