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J. Biol. Chem., Vol. 279, Issue 28, 29409-29417, July 9, 2004
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Stimulates p300-dependent RUNX3 Acetylation, Which Inhibits Ubiquitination-mediated Degradation*
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From the
Departments of Biochemistry and Urology, School of Medicine and Institute for Tumor Research, Chungbuk National University, Cheongju 361–763, South Korea
The Runt domain transcription factors (RUNXs) play essential roles in normal development and neoplasias. Genetic analyses of animals and humans have revealed the involvement of RUNX1 in hematopoiesis and leukemia, RUNX2 in osteogenesis and cleidocranial dysplasia, and RUNX3 in the development of T-cells and dorsal root ganglion neurons and in the genesis of gastric cancer. Here we report that RUNX3 is a target of the acetyltransferase activity of p300. The p300-dependent acetylation of three lysine residues protects RUNX3 from ubiquitin ligase Smurf-mediated degradation. The extent of the acetylation is up-regulated by the transforming growth factor-
signaling pathway and down-regulated by histone deacetylase activities. Our findings demonstrate that the level of RUNX3 protein is controlled by the competitive acetylation and deacetylation of the three lysine residues, revealing a new mechanism for the posttranslational regulation of RUNX3 expression.
Received for publication, December 2, 2003 , and in revised form, May 7, 2004.
* This work was supported by the Creative Research Program (M10301000012) and Proteomics Research Program (FRP-02-A-3) of the Ministry of Science and Technology of Korea (to S.-C. B.). 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. Tel.: 82-43-261-3457; Fax: 82-43-274-8705; E-mail: ginsenoside{at}runx3.co.kr. || To whom correspondence may be addressed. Tel.: 82-43-261-2842; Fax: 82-43-274-8705; E-mail: scbae{at}med.chungbuk.ac.kr.
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