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J. Biol. Chem., Vol. 280, Issue 22, 21427-21436, June 3, 2005

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Phosphorylation by the DHIPK2 Protein Kinase Modulates the Corepressor Activity of Groucho^*

Cheol Yong Choi¶, Young Ho Kim||, Yong-Ou Kim, Sang Joon Park, Eun-A Kim, William Riemenschneider, Kathleen Gajewski**, Robert A. Schulz**, and Yongsok Kim

From the Laboratory Research program, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, the Department of Biological Science, Sungkyunkwan University, 300 Chunchundong, Suwon 440-746, Korea, ^||Digital Biotech, 1227 Shingildong, Ansan 425-839, Korea, and the ^**Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, Texas 77030

Groucho function is essential for Drosophila development, acting as a corepressor for specific transcription factors that are downstream targets of various signaling pathways. Here we provide evidence that Groucho is phosphorylated by the DHIPK2 protein kinase. Phosphorylation modulates Groucho corepressor activity by attenuating its protein-protein interaction with a DNA-bound transcription factor. During eye development, DHIPK2 modifies Groucho activity, and eye phenotypes generated by overexpression of Groucho differ depending on its phosphorylation state. Moreover, analysis of nuclear extracts fractionated by column chromatography further shows that phospho-Groucho associates poorly with the corepressor complex, whereas the unphosphorylated form binds tightly. We propose that Groucho phosphorylation by DHIPK2 and its subsequent dissociation from the corepressor complex play a key role in relieving the transcriptional repression of target genes regulated by Groucho, thereby controlling cell fate determination during development.

Received for publication, January 14, 2005 , and in revised form, March 30, 2005.

^* This work was supported by the NHLBI Intramural Research Program (to Y. K.) and by Korea Research Foundation Grant KRF-2002-015-CP0313 (to C. Y. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¶ To whom correspondence may be addressed. E-mail: choicy{at}skku.ac.kr. To whom correspondence may be addressed. E-mail: yongsok{at}helix.nih.gov.

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