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Cossu, F.* ; Virili, S.* ; Braggiotti, B.* ; Bonì, F.* ; Ballabio, F. ; Giorgino, T.* ; Milani, M.* ; Mei, G.* ; Di Venere, A.* ; Mastrangelo, E.*

Structural dynamics and pH-regulated membrane binding of the TRAF2-NC trimer.

Protein Sci. 35:e70817 (2026)
Verlagsversion Forschungsdaten DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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
Zeitschrift Protein Science
Quellenangaben Band: 35, Heft: 11, Seiten: , Artikelnummer: e70817 Supplement: ,
Verlag Wiley
Verlagsort 111 River St, Hoboken 07030-5774, Nj Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
Förderungen Fondazione AIRC per la ricerca sul cancro ETS
Ministero dell'Universit e della Ricerca