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Molecular and Cellular Biology, July 2002, p. 5203-5211, Vol. 22, No. 14
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.14.5203-5211.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Novel Transcription Coactivator Complex Containing Activating Signal Cointegrator 1

Dong-Ju Jung,1 Hee-Sook Sung,2 Young-Wha Goo,1 Hyun Mi Lee,2 Ok Ku Park,2 Sung-Yun Jung,2 Janghoo Lim,2 Han-Jong Kim,2 Soo-Kyung Lee,1,3 Tae Sung Kim,4 Jae Woon Lee,1* and Young Chul Lee2*

Department of Life Science, Pohang University of Science and Technology, Pohang 790-784,1 Hormone Research Center,2 College of Pharmacy, Chonnam National University, Kwangju 500-757, Korea,3 Gene Expression Laboratory, Salk Institute of Biological Sciences, San Diego, California 920374

Received 27 February 2002/ Accepted 14 March 2002

Human activating signal cointegrator 1 (hASC-1) was originally isolated as a transcriptional coactivator of nuclear receptors. Here we report that ASC-1 exists as a steady-state complex associated with three polypeptides, P200, P100, and P50, in HeLa nuclei; stimulates transactivation by serum response factor (SRF), activating protein 1 (AP-1), and nuclear factor {kappa}B (NF-{kappa}B) through direct binding to SRF, c-Jun, p50, and p65; and relieves the previously described transrepression between nuclear receptors and either AP-1 or NF-{kappa}B. Interestingly, ectopic expression of Caenorhabditis elegans ASC-1 (ceASC-1), an ASC-1 homologue that binds P200 and P100, like hASC-1, while weakly interacting only with p65, in HeLa cells appears to replace endogenous hASC-1 from the hASC-1 complex and exerts potent dominant-negative effects on AP-1, NF-{kappa}B, and SRF transactivation. In addition, neutralization of endogenous P50 by single-cell microinjection of a P50 antibody inhibits AP-1 transactivation; the inhibition is relieved by coexpression of wild-type P50, but not of P50{Delta}KH, a mutant form that does not interact with P200. Overall, these results suggest that the endogenous hASC-1 complex appears to play an essential role in AP-1, SRF, and NF-{kappa}B transactivation and to mediate the transrepression between nuclear receptors and either AP-1 or NF-{kappa}B in vivo.

* Corresponding author. Mailing address for Jae Woon Lee: Department of Life Science, Pohang University of Science and Technology, Pohang 790-784, Korea. Phone: 82-54-279-2129. Fax: 82-54-279-8374. E-mail: jaewoon{at}postech.ac.kr. Mailing address for Young Chul Lee: Hormone Research Center, Chonnam National University, Kwangju 500-757, Korea. Phone: 82-62-530-0909. Fax: 82-62-530-0500. E-mail: yclee{at}chonnam.chonnam.ac.kr.

Molecular and Cellular Biology, July 2002, p. 5203-5211, Vol. 22, No. 14
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.14.5203-5211.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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