A novel TNF receptor-associated factor 6 binding domain mediates NF-kappa B signaling by the common cytokine receptor beta subunit.

The Journal of Immunology : Official Journal of the American Association of Immunologists
Mark B MeadsWilliam S Dalton

Abstract

GM-CSF, IL-3, and IL-5 are proinflammatory cytokines that control the production and function of myeloid and lymphoid cells. Their receptors are composed of a ligand-specific alpha subunit and a shared common signal-transducing beta subunit (beta common receptor or GM-CSFR beta [beta(c)]). The pleiotropic nature of biologic outcomes mediated by beta(c) and the presence of large, uncharacterized regions of its cytoplasmic domain suggest that much remains to be learned about its downstream signaling pathways. Although some previous work has attempted to link beta(c) with NF-kappaB activation, a definitive mechanism that mediates this pathway has not been described and, to date, it has not been clear whether the receptor can directly activate NF-kappaB. We demonstrate that NF-kappaB activation by beta(c) is dependent on TNFR-associated factor 6 (TRAF6) and that association of TRAF6 with beta(c) requires a consensus-binding motif found in other molecules known to interact with TRAF6. Furthermore, point mutation of this motif abrogated the ability of beta(c) to mediate NF-kappaB activation and reduced the viability of an IL-3-dependent hematopoietic cell line. Because this receptor plays a key role in hematopoiesis and the beta(c) c...Continue Reading

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Citations

Oct 4, 2011·Cellular and Molecular Life Sciences : CMLS·Megumi InomataTakeshi Into
Aug 11, 2011·PloS One·Hanif Javanmard KhamenehChristiane Ruedl
Dec 21, 2011·Molecular Medicine·Michael Brines, Anthony Cerami
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Oct 22, 2020·Phytomedicine : International Journal of Phytotherapy and Phytopharmacology·Tianle ZhanLingyan Zheng

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