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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.
Taken all together, Helicobacter pylori toxin Tip-alpha might activate NF-kappaB (show NFKB1 Proteins) to promote inflammation and carcinogenesis by inhibiting miR (show MLXIP Proteins)-3178 expression, which directly targets TRAF3, during Helicobacter pylori infection in gastric mucosal epithelial cells.
OPN (show SPP1 Proteins) acts as a positive regulator in innate antiviral immunity through stabilization of TRAF3.
PLK1 overexpression in prostate epithelial cells triggers oncogenic transformation. The signaling mechanisms underlying the observed cellular effects of PLK1 involve direct PLK1-dependent phosphorylation of CRAF with subsequent stimulation of the MEK1/2-ERK1/2-Fra1-ZEB1/2 signaling pathway.
These findings suggest that RNF166 positively regulates RNA virus-triggered IFN-beta (show IFNB1 Proteins) production by enhancing the ubiquitination of TRAF3 and TRAF6 (show TRAF6 Proteins).
Findings establish CK1varepsilon as a regulator of antiviral innate immune responses and indicate a novel mechanism of immunoregulation that involves CK1varepsilon-mediated phosphorylation of TRAF3.
findings identify TRAF3 and PTPN22 (show PTPN22 Proteins) as inhibitors of IL-6R signaling in B cells and reveal a previously uncharacterized role for TRAF3 in the regulation of plasma cell differentiation
TRAF3 regulates B-cell survival via inhibition of CREB (show CREB1 Proteins) stability
ESR1 (show ESR1 Proteins) directly interacts with TRAF3 and promotes K48-linked proteasomal degradation of TRAF3.
these findings demonstrate that WDR82 (show WDR82 Proteins) is a negative regulator of virus-triggered type I IFNs pathway through mediating TRAF3 polyubiquitination status and stability on mitochondria.
Hepatocyte TRAF3 promotes liver steatosis and insulin (show INS Proteins) resistance through targeting TAK1 (show NR2C2 Proteins)-dependent signaling.
TRAF3 expressed in myeloid cells regulates immune responses in myeloid cells and acts to inhibit inflammation and tumor development in mice.
The MYSM1 (show MYSM1 Proteins) SWIRM domain interacts with TRAF3 to terminate PRR (show PVRL1 Proteins) pathways for pro-inflammatory and type I interferon (show IFNA Proteins) responses.
Data show that the degradation of TNF receptor-associated factor 3 (TRAF3) and TNF (show TNF Proteins) receptor-associated Ffactor 6 (TRAF6 (show TRAF6 Proteins)) was accelerated in ubiquitin-specific protease 25 (show USP25 Proteins) knockout (USP25 (show USP25 Proteins)-/-) cells after viral infection.
Maternal diabetes and high glucose negatively regulate miR (show MLXIP Proteins)-322 through oxidative stress. miR (show MLXIP Proteins)-322 interacts with the 3'-UTR of TRAF3 and represses its translation.
These results indicate that the involvement of TRAF3 in IL-15 (show IL15 Proteins) mediated signaling to T cells plays a previously unappreciated and critical role in CD8 (show CD8A Proteins)+ central memory T cells regulation and maintenance.
TRAF3 is a central regulator of ischemic pathways, including nuclear factor kappaB, Rac-1, and c-Jun (show JUN Proteins) kinase (show MAPK9 Proteins) signaling, via its interaction with and activation of TAK1 (show NR2C2 Proteins).
Tumor necrosis factor (show TNF Proteins) receptor-associated factor 3 (TRAF3) is a positive regulator of pathological cardiac hypertrophy in mice and humans.
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 (TNFR) superfamily. This protein participates in the signal transduction of CD40, a TNFR family member important for the activation of the immune response. This protein is found to be a critical component of the lymphotoxin-beta receptor (LTbetaR) signaling complex, which induces NF-kappaB activation and cell death initiated by LTbeta ligation. Epstein-Barr virus encoded latent infection membrane protein-1 (LMP1) can interact with this and several other members of the TRAF family, which may be essential for the oncogenic effects of LMP1. Several alternatively spliced transcript variants encoding three distinct isoforms have been reported.
CD40 associated protein 1
, CD40 binding protein
, CD40 receptor associated factor 1
, LMP1-associated protein 1
, CD40 receptor-associated factor 1
, TNF receptor-associated factor 3