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Molecular & Cellular Proteomics 4:975-983, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Post-translational Modification of Nuclear Co-repressor Receptor-interacting Protein 140 by Acetylation^*

M. D. Mostaqul Huq and Li-Na Wei

From the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

Receptor-interacting protein 140 (RIP140) is a versatile co-regulator for nuclear receptors and many transcription factors and contains several autonomous repressive domains. RIP140 can be acetylated, and acetylation affects its biological activity. In this study, a comprehensive proteomic analysis using liquid chromatography-tandem mass spectroscopy was conducted to identify the in vivo acetylation sites on RIP140 purified from Sf21 insect cells. Eight acetylation sites were found within the amino-terminal and the central regions, including Lys¹¹¹, Lys¹⁵⁸, Lys²⁸⁷, Lys³¹¹, Lys⁴⁸², Lys⁵²⁹, Lys⁶⁰⁷, and Lys⁹³². Reporter assays were conducted to examine the effects of acetylation on various domains of RIP140. Green fluorescent protein-tagged fusion proteins were used to demonstrate the effect on nuclear translocation of these domains. A general inhibitor of reversible protein deacetylation was used to enrich the acetylated population of RIP140. The amino-terminal region (amino acids (aa) 1–495) was more repressive and accumulated more in the nuclei under hyperacetylated conditions, whereas hyperacetylation reduced the repressive activity and nuclear translocation of the central region (aa 336–1006). The deacetylase inhibitor had no effect on the carboxyl-terminal region (aa 977–1161) where no acetylation sites were found. Hyperacetylation also enhanced the repressive activity of the full-length protein but triggered its export into the cytosol in a small population of cells. This study revealed differential effects of post-translational modification on various domains of RIP140 through acetylation, including its effects on repressive activity and nuclear translocation of the full-length protein and its subdomains.

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