TRAF3
TRAF3 (TNF receptor-associated factor 3, also known as CAP-1, CD40bp, CRAF1, LAP1 and RNF118) is a cytoplasmic RING-type E3 ubiquitin ligase. It regulates NF-κB, MAPK and IRF signalling in both immune and non-immune cells. Browse Assay Genie's current range of TRAF3 research reagents below, or read on for the biology behind the target.
TRAF3 is a cytoplasmic E3 ubiquitin ligase that controls the NF-κB, mitogen-activated protein kinase (MAPK) and interferon regulatory factor (IRF) pathways, and through them a wide range of biological processes. In TLR and RLR signalling it promotes the synthesis of Lys-63-linked polyubiquitin chains on substrates such as ASC, leading to the type I interferon response or inflammasome activation. After activation of certain TLRs, including TLR4, it acts as a negative NF-κB regulator, possibly to limit unregulated inflammation. Its degradation through Lys-48-linked polyubiquitination is then required for MAPK activation and inflammatory cytokine production. When TLR4 drives bacterial expulsion, TRAF3 undergoes Lys-33-linked polyubiquitination and binds RALGDS, mobilising the exocyst complex to expel intracellular bacteria.
TRAF3 is a constitutive negative regulator of the alternative NF-κB pathway, which governs B-cell survival and lymphoid organ development. It down-regulates proteolytic processing of NFKB2, which inhibits non-canonical NF-κB activation, and promotes ubiquitination and proteasomal degradation of MAP3K14. The protein is required for normal antibody isotype switching from IgM to IgG and contributes to T-cell dependent immune responses. It is also involved in regulating the antiviral response.
The TRAF3 gene encodes a member of the TNF receptor-associated factor family, whose proteins associate with and transduce signals from members of the TNF receptor superfamily. TRAF3 participates in CD40 signalling and is a critical component of the lymphotoxin-beta receptor signalling complex, which induces NF-κB activation and cell death. Epstein-Barr virus LMP1 can interact with TRAF3 and other TRAF proteins, which may be essential for its oncogenic effects. Mutations in the gene are associated with herpes-specific infection-induced acute encephalopathy. The mouse ortholog is Traf3.
TRAF3 drives Lys-63-linked ubiquitination in TLR and RLR pathways, leading to type I interferon responses or inflammasome activation.
TRAF3 restrains the alternative NF-κB pathway by limiting NFKB2 processing and driving MAP3K14 degradation.
TRAF3 influences B-cell survival, lymphoid organ development and the switch from IgM to IgG antibody production.
TRAF3 supports antiviral responses, interacts with Epstein-Barr virus LMP1, and is linked to herpes-specific infection-induced encephalopathy.
TRAF3 is a cytoplasmic E3 ubiquitin ligase that regulates NF-κB, MAPK and IRF signalling. It promotes Lys-63-linked ubiquitination in TLR and RLR pathways, restrains the alternative NF-κB pathway, and is needed for IgM to IgG isotype switching.
TRAF3 is also called CAP-1, CD40bp, CRAF1, LAP1 and RNF118. The name CD40bp reflects its role in CD40 signalling. HGNC classes it among RING finger proteins, TNF receptor associated factors and RING finger E3 ubiquitin protein ligases.
Mutations in the TRAF3 gene are associated with herpes-specific, infection-induced acute encephalopathy. LMP1 of Epstein-Barr virus interacts with TRAF3. A mouse ortholog, Traf3, exists; check the datasheet of any product for its validated reactivity.
Other TNF receptor associated factors involved in TNFR family and NF-κB signalling, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13114; product specifications from Assay Genie datasheets.