Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor alpha

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Molecular and Cellular Biology, August 1999, p. 5363-5372, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor $alpha$

Hideki Endoh,¹^,² Kazunori Maruyama,¹ Yoshikazu Masuhiro,² Yoko Kobayashi,² Masahide Goto,¹ Hitoshi Tai,² Junn Yanagisawa,² Daniel Metzger,³ Seiichi Hashimoto,¹ and Shigeaki Kato²^,⁴^,^*

Molecular Medicine Laboratories, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical, Tsukuba, Ibaraki 305-8585,¹ Institute for Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032,² and CREST, Japan Science and Technology, Kawaguchi, Saitama 332-0012,⁴ Japan, and Institut de Genetique et de Biologie Moleculaire et Cellulaire, (IGBMC)/CNRS/INSERM/ULP College de France, 67404 Illkirch Cedex, C.U. de Strasbourg, France³

Received 19 January 1999/Returned for modification 1 March 1999/Accepted 5 May 1999

The estrogen receptor (ER) regulates the expression of target genes in a ligand-dependent manner. The ligand-dependent activationfunction AF-2 of the ER is located in the ligand binding domain(LBD), while the N-terminal A/B domain (AF-1) functions in a ligand-independentmanner when isolated from the LBD. AF-1 and AF-2 exhibit celltype and promoter context specificity. Furthermore, the AF-1 activityof the human ER $alpha$ (hER $alpha$ ) is enhanced through phosphorylation ofthe Ser¹¹⁸ residue by mitogen-activated protein kinase (MAPK). From MCF-7cells, we purified and cloned a 68-kDa protein (p68) which interactedwith the A/B domain but not with the LBD of hER $alpha$ . Phosphorylationof hER $alpha$ Ser¹¹⁸ potentiated the interaction with p68. We demonstrate that p68enhanced the activity of AF-1 but not AF-2 and the estrogen-inducedas well as the anti-estrogen-induced transcriptional activityof the full-length ER $alpha$ in a cell-type-specific manner. However,it did not potentiate AF-1 or AF-2 of ER $beta$ , androgen receptor,retinoic acid receptor alpha, or mineralocorticoid receptor. Wealso show that the RNA helicase activity previously ascribed top68 is dispensable for the ER $alpha$ AF-1 coactivator activity and thatp68 binds to CBP in vitro. Furthermore, the interaction regionfor p68 in the ER $alpha$ A/B domain was essential for the full activityof hER $alpha$ AF-1. Taken together, these findings show that p68 actsas a coactivator specific for the ER $alpha$ AF-1 and strongly suggestthat the interaction between p68 and the hER $alpha$ A/B domain is regulatedby MAPK-induced phosphorylation of Ser¹¹⁸.

^* Corresponding author. Mailing address: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1,Bunkyo-ku, Tokyo 113-0032, Japan. Phone: 81-3-5841-8478. Fax:81-3-5841-8477. E-mail: uskato{at}hongo.ecc.u-tokyo.ac.jp.

Molecular and Cellular Biology, August 1999, p. 5363-5372, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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