AI Article Synopsis
- TRAF1 is distinct from other TRAF family members because it doesn't have the typical RING/zinc-finger domain, and its specific functions remain uncertain due to conflicting research findings.
- TRAF1 has been shown to interact with the BAFF receptor and enhance the activation of the alternative NF-kappaB signaling pathway by stabilizing NIK and promoting the conversion of p100 to its mature form, p52.
- Reducing TRAF1 levels in a Hodgkin's disease cell line disrupts p100 processing and affects gene transcription linked to p52, indicating that TRAF1 is a key positive regulator in this pathway.
Article Abstract
Tumor necrosis factor receptor-associated factor 1 (TRAF1) is unique among the members of the TRAF family, as it lacks the N-terminal RING/zinc-finger domain. Also the function of TRAF1 is not clearly established, with many papers reporting contradictory results. Here we show that TRAF1 interacts with BAFF receptor, a member of the TNF receptor family, and positively regulates activation of the alternative NF-kappaB pathway. Ectopic expression of TRAF1 causes degradation of TRAF3, stabilization of NIK, and processing of p100 to produce the mature form p52. In addition, we show that knocking-down expression of TRAF1 in the Hodgkin's disease derived cell line L1236, interfere with p100 processing and with p52 mediate gene transcription. Collectively these results support a role for TRAF1 as a positive regulator of the NF-kappaB alternative pathway.
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| http://dx.doi.org/10.1016/j.molimm.2009.07.029 | DOI Listing |
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