Cancer Research The Future of Cancer Research: Science and Patient Impact AACR Conference on Molecular Diagnostics - 2008
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[Cancer Research 63, 6135-6139, October 1, 2003]
© 2003 American Association for Cancer Research

Advances in Brief

Menin, a Tumor Suppressor, Represses JunD-Mediated Transcriptional Activity by Association with an mSin3A-Histone Deacetylase Complex1

Hyungsoo Kim2, Ji-Eun Lee2, Eun-Jung Cho, Jun O. Liu and Hong-Duk Youn3

Department of Biochemistry and Molecular Biology, Cancer Research Institute, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea [H. K., J-E. L., H-D. Y.]; College of Pharmacy, Sungkyunkwan University, Suwon, 440-746 Republic of Korea [E-J. C.]; and Department of Pharmacology and Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 [J. O. L.]

Menin, a gene product of multiple endocrine neoplasia type I (MEN1), is known to act as a tumor suppressor to repress JunD transcription factor. However, the mechanism by which Menin represses JunD transcriptional activity was still unclear. In this study, we found that Menin is a corepressor against JunD transcriptional activity via recruitment of histone deacetylases in an mSin3A-dependent manner. The amino acid search revealed that central domain of Menin includes a {alpha}-helical mSin3-interacting domain [SID (371–387)]. The SID mutation of Menin (L381P/A385P) abolished the interaction between mSin3A and paired amphipathic helix 2 domain of Menin and reduced its ability to repress JunD transcriptional activity, implicating that SID of Menin is important for recruiting an mSin3A-histone deacetylase complex to repress JunD transcriptional activity.




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