TNF receptor-associated factors (TRAFs) are characterized by an oligomeric structure that plays a fundamental role in the binding process with membrane receptors. In this work, we studied the trimer-to-monomer (T ↔ 3M) equilibrium transition of the TRAF2 C-terminal domain using both chemical (dilution/guanidinium hydrochloride) and mechanical stress (high pressure) to induce the dissociation of the native protein into subunits. The experimental results and computer simulations indicate that stable monomers exist and that their population accounts for 15% of the total TRAF2 molecules already at a physiological intracellular concentration (≈1 μM), being instead the predominant species in the nanomolar concentration range. Because the total amount of TRAF2 changes during a cell cycle, the monomer-trimer equilibrium can be crucial for regulating the activities of TRAF2 in vivo.

Ceccarelli, A., DI VENERE, A., Nicolai, E., DE LUCA, A., Minicozzi, V., Rosato, N., et al. (2015). TNFR-Associated Factor-2 (TRAF2): Not only a Trimer. BIOCHEMISTRY, 54(40), 6153-6161 [10.1021/acs.biochem.5b00674].

TNFR-Associated Factor-2 (TRAF2): Not only a Trimer

DI VENERE, ALMERINDA;NICOLAI, ELEONORA;DE LUCA, ANASTASIA;MINICOZZI, VELIA;ROSATO, NICOLA;CACCURI, ANNA MARIA;MEI, GIAMPIERO
2015-01-01

Abstract

TNF receptor-associated factors (TRAFs) are characterized by an oligomeric structure that plays a fundamental role in the binding process with membrane receptors. In this work, we studied the trimer-to-monomer (T ↔ 3M) equilibrium transition of the TRAF2 C-terminal domain using both chemical (dilution/guanidinium hydrochloride) and mechanical stress (high pressure) to induce the dissociation of the native protein into subunits. The experimental results and computer simulations indicate that stable monomers exist and that their population accounts for 15% of the total TRAF2 molecules already at a physiological intracellular concentration (≈1 μM), being instead the predominant species in the nanomolar concentration range. Because the total amount of TRAF2 changes during a cell cycle, the monomer-trimer equilibrium can be crucial for regulating the activities of TRAF2 in vivo.
2015
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Ceccarelli, A., DI VENERE, A., Nicolai, E., DE LUCA, A., Minicozzi, V., Rosato, N., et al. (2015). TNFR-Associated Factor-2 (TRAF2): Not only a Trimer. BIOCHEMISTRY, 54(40), 6153-6161 [10.1021/acs.biochem.5b00674].
Ceccarelli, A; DI VENERE, A; Nicolai, E; DE LUCA, A; Minicozzi, V; Rosato, N; Caccuri, Am; Mei, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/130552
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