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and IFN-
as Modulators of TNF- Signaling in Macrophages: Regulation and Functional Implications of the TNF Receptor 1:STAT-1 Complex1
Department of Cell Biology, University of Alabama, Birmingham, AL 35294
TNF-
and IFN-
cooperate in the activation of macrophages. TNF--dependent activation of NF-
B is stronger in the presence of IFN-. STAT-1 associates with TNFR1 in TNF--treated cells, and this association attenuates TNF--mediated NF-B activation. We hypothesized that nuclear localization of STAT-1 due to IFN- signaling would preclude it from being recruited to the TNFR1 and therefore enhance TNF--induced NF-B activation. In the RAW264.7 macrophage cell line, TNF- treatment indeed recruits STAT-1 to the TNFR1, and this association is abrogated when cells are exposed to IFN-. TNF- treatment induces a more robust activation of NF-B in STAT-1-deficient cells, and restoration of STAT-1 inhibits TNF--dependent NF-B activation. Our results suggest that a receptor-proximal level of cross-talk exists between these two cytokine pathways: IFN- limits STAT-1 availability to the TNFR1 by depleting STAT-1 from the cytoplasm, thus allowing for optimal NF-B activation upon TNF- ligation.
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