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J. Biol. Chem., Vol. 281, Issue 20, 14417-14428, May 19, 2006

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Interactions between PIAS Proteins and SOX9 Result in an Increase in the Cellular Concentrations of SOX9^*

Takako Hattori¹, Heidi Eberspaecher, Jingfang Lu, Ren Zhang, Tamotsu Nishida, Tomoaki Kahyo, Hideyo Yasuda^¶, and Benoit de Crombrugghe²

From the Department of Molecular Genetics, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, the Division of Molecular Biology, School of Life Science, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan, and the ^¶Division of Bioscience, Central Laboratory, Nippon Flour Mills, Co., Ltd., 5-1-3 Midorigaoka, Atsugi, Kanagawa 243-0041, Japan

We have identified PIAS1 (protein inhibitor of activated STAT-1), -3, -x, and -x as SOX9-associated polypeptides using the Gal4-based yeast two-hybrid system and a cDNA library derived from a chondrocytic cell line. These PIAS proteins were shown to interact directly with SOX9 in two-hybrid, co-immunoprecipitation, and electrophoretic mobility shift assays. SOX9 was sumoylated in cotransfection experiments with COS-7 cells using PIAS and SUMO-1 (small ubiquitin-like modifier-1) expression vectors. SOX9 was also sumoylated in vitro by PIAS proteins in the presence of SUMO-1, the SUMO-activating enzyme, and the SUMO-conjugating enzyme. In COS-7 cells, PIAS proteins stimulated the SOX9-dependent transcriptional activity of a Col2a1 promoter-enhancer reporter. This increase in reporter activity was paralleled by an increase in the cellular levels of SOX9. Cotransfection with a SUMO-expressing vector further enhanced the transcriptional activity of this SOX9-dependent Col2a1 reporter in COS-7 cells, and this additional activation was inhibited in the presence of either SUMO-1 mutants or PIAS RING domain mutants or by coexpression of a desumoylation enzyme. Immunofluorescence microscopy of SOX9-transfected COS-7 cells showed that the subnuclear distribution of SOX9 became more diffuse in the presence of PIAS1 and SUMO-1. Our results suggest that, by controlling the cellular concentrations of SOX9, PIAS proteins and sumoylation may be part of a major regulatory system of SOX9 functions.

Received for publication, October 18, 2005 , and in revised form, March 21, 2006.

^* 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.

¹ Present address: Department of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8525, Japan.

² To whom correspondence should be addressed: Dept. of Molecular Genetics, University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030. Tel.: 713-834-6376; Fax: 713-834-6396; E-mail: bdecromb{at}mdanderson.org.

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