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Originally published In Press as doi:10.1074/jbc.M003409200 on June 1, 2000

J. Biol. Chem., Vol. 275, Issue 35, 27377-27385, September 1, 2000
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The Interferon- and Differentiation-inducible p202a Protein Inhibits the Transcriptional Activity of c-Myc by Blocking Its Association with Max*

Hong WangDagger , Chuan-ju LiuDagger , Yunbiao LuDagger , Gouri ChatterjeeDagger , Xian-Yong MaDagger , Robert N. Eisenman§, and Peter LengyelDagger ||

From the Dagger  Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 and the § Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104

p202a is a murine protein that is induced during the fusion of myoblasts to myotubes and can also be induced by interferon. Even 2-3-fold overexpression of p202a in cells retards proliferation. p202a was shown to modulate transcription by binding, and inhibiting the activity of several transcription factors including c-Fos, c-Jun, AP-2, E2F1, E2F4, NF-kappa B, MyoD, and myogenin. Here we report that p202a also bound the c-Myc protein in vitro and in vivo; the C-terminal p202a b segment bound the C-terminal basic region helix-loop-helix-leucine zipper (bHLHLZ) region of c-Myc. The transfection of a p202a expression plasmid inhibited the c-Myc-dependent expression of reporter plasmids in transient assays; moreover, overexpression of p202a in stable cell lines decreased the endogenous levels of mRNAs whose expression is driven by c-Myc. These effects of p202a are consistent with our finding that the binding of p202a to c-Myc inhibited the binding of c-Myc to Max in vitro and in vivo. p202a also inhibited the c-Myc-induced anchorage-independent growth and apoptosis of Rat-1 cells. The inhibition of c-Myc-dependent transcription, proliferation, and apoptosis by p202a is in line with the involvement of p202a in differentiation.

* This work was supported by a postdoctoral fellowship from the Cancer Research Institute (to H. W.) and NIAID, National Institutes of Health Research Grants R37-AI12320 (to P. L.) and CA20525 (to R. N. E).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

American Cancer Society Research Professor.

|| To whom correspondence should be addressed: Dept. of Molecular Biophysics and Biochemistry, Yale University, 333 Cedar St., New Haven, CT 06520. Tel.: 203-737-2061; Fax: 203-785-6404, E-mail: peter.lengyel@yale.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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