TNF Receptor-Associated Factor 6

2020 ◽  
Author(s):  
Keyword(s):  
Tnf Receptor ◽  
Associated Factor

scholarly journals The Odd Faces of Oligomers: The Case of TRAF2-C, A Trimeric C-Terminal Domain of TNF Receptor-Associated Factor

2021 ◽  
Vol 22 (11) ◽  
pp. 5871
Author(s):  
Almerinda Di Venere ◽  
Eleonora Nicolai ◽  
Velia Minicozzi ◽  
Anna Maria Caccuri ◽  
Luisa Di Paola ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Strong Dependence ◽  
Conformational Dynamics ◽  
Receptor Interaction ◽  
Tnf Receptor ◽  
Oligomeric State ◽  
Dynamic Simulations ◽  
Associated Factor ◽  
Terminal Domain

TNF Receptor Associated Factor 2 (TRAF2) is a trimeric protein that belongs to the TNF receptor associated factor family (TRAFs). The TRAF2 oligomeric state is crucial for receptor binding and for its interaction with other proteins involved in the TNFR signaling. The monomer-trimer equilibrium of a C- terminal domain truncated form of TRAF2 (TRAF2-C), plays also a relevant role in binding the membrane, causing inward vesiculation. In this study, we have investigated the conformational dynamics of TRAF2-C through circular dichroism, fluorescence, and dynamic light scattering, performing temperature-dependent measurements. The data indicate that the protein retains its oligomeric state and most of its secondary structure, while displaying a significative increase in the heterogeneity of the tyrosines signal, increasing the temperature from ≈15 to ≈35 °C. The peculiar crowding of tyrosine residues (12 out of 18) at the three subunit interfaces and the strong dependence on the trimer concentration indicate that such conformational changes mainly involve the contact areas between each pair of monomers, affecting the oligomeric state. Molecular dynamic simulations in this temperature range suggest that the interfaces heterogeneity is an intrinsic property of the trimer that arises from the continuous, asymmetric approaching and distancing of its subunits. Such dynamics affect the results of molecular docking on the external protein surface using receptor peptides, indicating that the TRAF2-receptor interaction in the solution might not involve three subunits at the same time, as suggested by the static analysis obtainable from the crystal structure. These findings shed new light on the role that the TRAF2 oligomeric state might have in regulating the protein binding activity in vivo.

scholarly journals Leukocyte-specific protein 1 links TNF receptor-associated factor 1 to survival signaling downstream of 4-1BB in T cells

2013 ◽  
Vol 93 (5) ◽  
pp. 713-721 ◽  
Author(s):  
Laurent Sabbagh ◽  
Daniela Andreeva ◽  
Geneviève Dubeau Laramée ◽  
N. A. Eustache Oussa ◽  
Déborah Lew ◽  
...  
Keyword(s):  
T Cells ◽  
Specific Protein ◽  
Tnf Receptor ◽  
Associated Factor ◽  
Survival Signaling

TNF Receptor–Associated Factor 5 Limits IL-27 Receptor Signaling in CD4+ T Lymphocytes

2022 ◽  
pp. ji2001358
Author(s):  
Eigo Kawahara ◽  
Mitsuki Azuma ◽  
Hiroyuki Nagashima ◽  
Koki Omori ◽  
Sho Akiyama ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Tnf Receptor ◽  
Receptor Signaling ◽  
Associated Factor

scholarly journals X-linked inhibitor of apoptosis-associated factor 1 regulates TNF receptor 1 complex stability

FEBS Letters ◽  
2016 ◽  
Vol 590 (23) ◽  
pp. 4381-4392 ◽  
Author(s):  
Boren Lin ◽  
Da Xu ◽  
Douglas W. Leaman
Keyword(s):  
Inhibitor Of Apoptosis ◽  
Complex Stability ◽  
Tnf Receptor ◽  
Associated Factor
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