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Originally published In Press as doi:10.1074/jbc.M004252200 on July 20, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31883-31890, October 13, 2000
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A Novel Cellular Protein (MTBP) Binds to MDM2 and Induces a G1 Arrest That Is Suppressed by MDM2*

Mark T. BoydDagger , Nikolina Vlatkovic§, and Dale S. Haines

From the Division of Hematology/Oncology, MCP Hahnemann University Cancer Center, Philadelphia, Pennsylvania 19102

The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. In addition to binding to and inhibiting the transcriptional activation function of the p53 protein, MDM2 binds, inter alia, to RB and the E2F-1·DP-1 complex and in so doing may promote progression of cells into S phase. Mice transgenic for Mdm2 possess cells that have cell cycle regulation defects and develop an altered tumor profile independent of their p53 status. MDM2 also blocks the growth inhibitory effects of transforming growth factor-beta 1 in a p53-independent manner. We show here that a novel growth regulatory molecule is also the target of MDM2-mediated inhibition. Using a yeast two-hybrid screen, we have identified a gene that encodes a novel cellular protein (MTBP) that binds to MDM2. MTBP can induce G1 arrest, which in turn can be blocked by MDM2. Our results suggest the existence of another growth control pathway that may be regulated, at least in part, by MDM2.

* This work was supported in part by grants from the Breast Health Institute of Philadelphia (to M. T. B.) and from the W. W. Smith Charitable Trust (to M. T. B. and D. S. H.), by National Institutes of Health Grant CA70165 (to D. S. H.), and by the Institute for Cancer and Blood Diseases, Hahnemann University Hospital.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ278508.

Dagger To whom correspondence should be addressed: Dept. of Surgery, University of Liverpool, Daulby St., Liverpool L69 3GA, UK. Tel.: 44-151-706-4185; Fax: 44-151-706-5826; E-mail: mboyd@liverpool.ac.uk.

§ Present address: Dept. of Surgery, University of Liverpool, Liverpool L69 3GA, UK.

Present address: Fels Inst., Temple University School of Medicine, Philadelphia, PA 19140.

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