title: TNFR-Associated Factor-2 (TRAF2): Not Only a Trimer.
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.
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.
authors.forename: Arianna
authors.initials: A
authors.lastname: Ceccarelli
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Almerinda
authors.initials: A
authors.lastname: Di Venere
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Eleonora
authors.initials: E
authors.lastname: Nicolai
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Anastasia
authors.initials: A
authors.lastname: De Luca
authors.affiliation: Physics Department, INFN University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Velia
authors.initials: V
authors.lastname: Minicozzi
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Nicola
authors.initials: N
authors.lastname: Rosato
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Anna Maria
authors.initials: AM
authors.lastname: Caccuri
authors.affiliation: Department of Experimental Medicine and Surgery, University of Rome Tor Vergata , Via Montpellier 1, 00133 Rome, Italy.|The NAST Centre for Nanoscience & Nanotechnology & Innovative Instrumentation, University of Rome Tor Vergata , Via della Ricerca Scientifica 1, 00133 Rome, Italy.
authors.forename: Giampiero
authors.initials: G
authors.lastname: Mei
mesh_terms: D002460:Cell Line; D006801:Humans; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D055550:Protein Stability; D047992:TNF Receptor-Associated Factor 2 / Q000032:analysis / Q000737:chemistry*
chemical_list: D047992:TNF Receptor-Associated Factor 2