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Results showed that high expression of TRAF2 was significantly associated with tumor stage of prostate cancer.
The addition of nanomolar concentration of TRAF2 in GUVs also seems to exert a mechanical action.
TRAF2 and OTUD7B (show OTUD7B Proteins) govern a ubiquitin-dependent switch that regulates mTORC2 (show CRTC2 Proteins) signalling
destabilization of TRAF2 by miR-17 reduced the ability of TRAF2 to associate with cIAP2 (show BIRC3 Proteins), resulting in the downregulation of TNF-alpha (show TNF Proteins)-induced NF-kappaBp65, c-Jun (show JUN Proteins), and STAT3 (show STAT3 Proteins) nuclear translocation and the production of IL-6 (show IL6 Proteins), IL-8 (show IL8 Proteins), MMP-1 (show MMP1 Proteins), and MMP-13 (show MMP13 Proteins) in human rheumatoid arthritis synovial fibroblasts.
HOXA1 (show HOXA1 Proteins)-mediated activation of NF-kappaB (show NFKB1 Proteins) is non-transcriptional and the RBCK1 (show RBCK1 Proteins) and TRAF2 influences on NF-kappaB (show NFKB1 Proteins) are epistatic to HOXA1 (show HOXA1 Proteins)
RIPK1 (show RIPK1 Proteins) collaborates with TRAF2 to inhibit murine and human hepatocarcinogenesis.
Data suggest that TRAF2 (TNF receptor-associated factor 2) negatively regulates (1) TNFR1- (tumor necrosis factor binding protein 1 (show TNFRSF1A Proteins))-induced apoptosis, (2) TNFR2 (show TNFRSF1B Proteins)- (tumor necrosis factor (show TNF Proteins) receptor type 2)-induced non-canonical NFkappaB (show NFKB1 Proteins) signaling, and (3) TNF- (tumor necrosis factor (show TNF Proteins))-induced necroptosis. [REVIEW]
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.
work reveals that simulated microgravity promotes the apoptotic response through a combined modulation of the Uev1A/TICAM/TRAF (show TRAF1 Proteins)/NF-kappaB (show NFKB1 Proteins)-regulated apoptosis and the p53 (show TP53 Proteins)/PCNA (show PCNA Proteins)- and ATM (show ATM Proteins)/ATR-Chk1 (show CHEK1 Proteins)/2-controlled DNA-damage response pathways.
Traf2 mediates the pro-survival pathway in the heart by suppressing necroptotic signaling.
Targeting TRAF2 may be useful as a therapeutic approach for immunosuppression-free islet allograft survival that avoids the thromboembolic complications associated with the use of anti-CD40L (show CD40LG Proteins) antibodies.
Celastrol promotes Nur77 (show NR4A1 Proteins) migration from the nucleus to mitochondria, where it is ubiquitinated by TRAF2. Ubiquitinated Nur77 (show NR4A1 Proteins) then interacts with p62/SQSTM1 (show SQSTM1 Proteins), leading to autophagy of dysfunctional mitochondria and alleviation of inflammation.
this study shows that TRAF2 and TRAF5 (show TRAF5 Proteins) work as important regulators of the IL-6R signaling needed for Th17 development
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
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