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Study presents the characterization of the peptide binding preferences of TRAFs 2, 3, and 5 using deep mutational scanning. The three TRAF (show TRAF1 Proteins) proteins demonstrated different preferences for binding to members of the CD40 (show CD40 Proteins) library, and three peptides from that library individually showed striking differences in affinity for the three TRAFs.
The data demonstrate a novel and unexpected function of BIG1 that regulates TNFR1 (show TNFRSF1A Proteins) signaling by targeting TRAF2.
TRAF2 expression was increased in gastric cancer patients as a result of DNA hypomethylation.
Data show that when death receptor 5 (DR5 (show TNFRSF10B Proteins)) is suppressed, caspase-8 (show CASP8 Proteins) may recruit and stabilize TNF receptor-associated factor 2 (TRAF2) to form a metastasis and invasion signaling complex, resulting in activation of ERK (show EPHB2 Proteins) signaling.
these findings reveal a novel mechanism by which TRAF2 mediates Lys63-linked ubiquitination of DUSP14 (show DUSP14 Proteins), leading to DUSP14 (show DUSP14 Proteins) activation in T cells
There was a significant positive correlation between TRAF2 and TRAF4 (show TRAF4 Proteins) expression levels in malignant pleural effusion cells
Data show that ectopic expression of interferon regulatory factor 1 (IRF-1 (show IRF1 Proteins)) reduces NF-kappa B (show NFKB1 Proteins) activity and suppresses TNF receptor-associated factor 2 (TRAF2) and inhibitor of apoptosis 1 (show BIRC2 Proteins) protein (cIAP1 (show BIRC2 Proteins)) expression in breast cancer cells.
The results identify TRAF2 as an important biological suppressor of necroptosis in vitro and in vivo.
MAVS50, exposing a degenerate TRAF (show TRAF1 Proteins)-binding motif within its N-terminus, effectively competed with full-length MAVS (show MAVS Proteins) for recruiting TRAF2 and TRAF6 (show TRAF6 Proteins)
Presented is the trimer-to-monomer 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.
Keratinocyte-specific deletion of Traf2, but not Sphk1 (show SPHK1 Proteins) deficiency, disrupted TNF (show TNF Proteins) mediated NF-kappaB (show NFKB1 Proteins) and MAP kinase (show MAPK1 Proteins) signalling and caused epidermal hyperplasia and psoriatic skin inflammation.
TRAF2 functions as a key activator of MST1 (show MST1 Proteins) in oxidative stress-induced (show SQSTM1 Proteins) intracellular signaling processes.
Proinflammatory TLR signalling is regulated by a TRAF2-dependent proteolysis mechanism in macrophages.
NFkappaB anti-apoptotic target genes TNF receptor-associated factor 1 (TRAF1 (show TRAF1 Proteins)), TNF receptor-associated factor 2 (TRAF2), cellular inhibitor of apoptosis (cIAP2 (show BIRC3 Proteins)), and Ferritin heavy chain (FTH1 (show FTH1 Proteins)) were increased following Losartan treatment
These studies demonstrate a critical role for TRAF2 in the maintenance of peripheral CD8 (show CD8A Proteins)(+) CD44 (show CD44 Proteins)(hi) CD122 (show IL2RB Proteins)(+) T-cell and NKT (show CTSL1 Proteins)-cell homeostasis by modulating sensitivity to T-cell intrinsic growth factors such as IL-15 (show IL15 Proteins).
HGK/MAP4K4 (show MAP4K4 Proteins) deficiency has a role in inducing TRAF2 stabilization and Th17 differentiation leading to insulin (show INS Proteins) resistance
identifying the CYLD (show CYLD Proteins)-TRAF2-p38MAPK (show MAPK14 Proteins) pathway as a novel important regulator of HSC (show FUT1 Proteins) function restricting HSC (show FUT1 Proteins) cycling and promoting dormancy.
Data indicate that caspase-8 (show CASP8 Proteins) activity is lost upon deletion of c-FLIPL (show CFLAR Proteins), and p43FLIP rescues caspase-8 (show CASP8 Proteins) activity through Raf1 (show RAF1 Proteins), TRAF2, and RIPK1 (show RIPK1 Proteins) association, augmenting ERK (show EPHB2 Proteins) and NF-kappaB (show NFKB1 Proteins) pathways
IpaH0722 dampens the acute inflammatory response by preferentially inhibiting the PKC-mediated activation of NF-kappaB by ubiquitinating TRAF2, a molecule downstream of PKC, and by promoting its proteasome-dependent degradation.
Data indicate that deletion of Tnfr1 (show TNFRSF1A Proteins) gene more efficiently decreased the percentages of IL-10 (show IL10 Proteins)-secreting neutrophils in PB and BM cells from tumor necrosis factor (TNF (show TNF Proteins)) receptor-associated factor (Traf)2(-/-) mice.
The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from members of the TNF receptor superfamily. This protein directly interacts with TNF receptors, and forms a heterodimeric complex with TRAF1. This protein is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF1 interacts with the inhibitor-of-apoptosis proteins (IAPs), and functions as a mediator of the anti-apoptotic signals from TNF receptors. The interaction of this protein with TRADD, a TNF receptor associated apoptotic signal transducer, ensures the recruitment of IAPs for the direct inhibition of caspase activation. BIRC2/c-IAP1, an apoptosis inhibitor possessing ubiquitin ligase activity, can unbiquitinate and induce the degradation of this protein, and thus potentiate TNF-induced apoptosis. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of only one transcript has been determined.
, conjugal transfer protein TraF
, E3 ubiquitin-protein ligase TRAF2
, tumor necrosis factor type 2 receptor associated protein 3
, tumor necrosis factor type 2 receptor-associated protein 3
, TRAF family member-associated NFKB activator
, TNF receptor-associated factor 2