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Molecular and Cellular Biology, May 2002, p. 3549-3561, Vol. 22, No. 10
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.10.3549-3561.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator Activity by I{kappa}B Kinase

Ray-Chang Wu, Jun Qin, Yoshihiro Hashimoto, Jiemin Wong, Jianming Xu, Sophia Y. Tsai, Ming-Jer Tsai, and Bert W. O'Malley*

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030

Received 23 October 2001/ Returned for modification 17 December 2001/ Accepted 15 February 2002

In the past few years, many nuclear receptor coactivators have been identified and shown to be an integral part of receptor action. The most frequently studied of these coactivators are members of the steroid receptor coactivator (SRC) family, SRC-1, TIF2/GRIP1/SRC-2, and pCIP/ACTR/AIB-1/RAC-3/TRAM-1/SRC-3. In this report, we describe the biochemical purification of SRC-1 and SRC-3 protein complexes and the subsequent identification of their associated proteins by mass spectrometry. Surprisingly, we found association of SRC-3, but not SRC-1, with the I{kappa}B kinase (IKK). IKK is known to be responsible for the degradation of I{kappa}B and the subsequent activation of NF-{kappa}B. Since NF-{kappa}B plays a key role in host immunity and inflammatory responses, we therefore investigated the significance of the SRC-3-IKK complex. We demonstrated that SRC-3 was able to enhance NF-{kappa}B-mediated gene expression in concert with IKK. In addition, we showed that SRC-3 was phosphorylated by the IKK complex in vitro. Furthermore, elevated SRC-3 phosphorylation in vivo and translocation of SRC-3 from cytoplasm to nucleus in response to tumor necrosis factor alpha occurred in cells, suggesting control of subcellular localization of SRC-3 by phosphorylation. Finally, the hypothesis that SRC-3 is involved in NF-{kappa}B-mediated gene expression is further supported by the reduced expression of interferon regulatory factor 1, a well-known NF-{kappa}B target gene, in the spleens of SRC-3 null mutant mice. Taken together, our results not only reveal the IKK-mediated phosphorylation of SRC-3 to be a regulated event that plays an important role but also substantiate the role of SRC-3 in multiple signaling pathways.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-6205. Fax: (713) 798-5599. E-mail: berto{at}bcm.tmc.edu.

Molecular and Cellular Biology, May 2002, p. 3549-3561, Vol. 22, No. 10
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.10.3549-3561.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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