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Molecular and Cellular Biology, July 1999, p. 4798-4805, Vol. 19, No. 7
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Activation of Phosphatidylinositol 3-Kinase in Response to Interleukin-1 Leads to Phosphorylation and Activation of the NF-kappa B p65/RelA Subunit

Nywana Sizemore,1 Stewart Leung,2 and George R. Stark1,*

Department of Molecular Biology, Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, Ohio 44195,1 and Department of Immunology, Berlex Biosciences, Richmond, California 948042

Received 16 November 1998/Returned for modification 11 January 1999/Accepted 5 April 1999

The work of Reddy et al. (S. A. Reddy, J. A. Huang, and W. S. Liao, J. Biol. Chem. 272:29167-29173, 1997) reveals that phosphatidylinositol 3-kinase (PI3K) plays a role in transducing a signal from the occupied interleukin-1 (IL-1) receptor to nuclear factor kappa B (NF-kappa B), but the underlying mechanism remains to be determined. We have found that IL-1 stimulates interaction of the IL-1 receptor accessory protein with the p85 regulatory subunit of PI3K, leading to the activation of the p110 catalytic subunit. Specific PI3K inhibitors strongly inhibit both PI3K activation and NF-kappa B-dependent gene expression but have no effect on the IL-1-stimulated degradation of Ikappa Balpha , the nuclear translocation of NF-kappa B, or the ability of NF-kappa B to bind to DNA. In contrast, PI3K inhibitors block the IL-1-stimulated phosphorylation of NF-kappa B itself, especially the p65/RelA subunit. Furthermore, by using a fusion protein containing the p65/RelA transactivation domain, we found that overexpression of the p110 catalytic subunit of PI3K induces p65/RelA-mediated transactivation and that the specific PI3K inhibitor LY294,002 represses this process. Additionally, the expression of a constitutively activated form of either p110 or the PI3K-activated protein kinase Akt also induces p65/RelA-mediated transactivation. Therefore, IL-1 stimulates the PI3K-dependent phosphorylation and transactivation of NF-kappa B, a process quite distinct from the liberation of NF-kappa B from its cytoplasmic inhibitor Ikappa B.

* Corresponding author. Mailing address: Lerner Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Phone: (216) 444-3900. Fax: (216) 444-3279. E-mail: starkg{at}cesmtp.ccf.org.

Molecular and Cellular Biology, July 1999, p. 4798-4805, Vol. 19, No. 7
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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