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J. Biol. Chem., Vol. 275, Issue 43, 33607-33613, October 27, 2000
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From the Insulin-like growth factor-binding protein
(IGFBP)-3 regulates apoptosis in an IGF-independent fashion and has
been shown to localize to nuclei. We cloned the nuclear receptor
retinoid X receptor-
Direct Functional Interactions between Insulin-like Growth
Factor-binding Protein-3 and Retinoid X Receptor-
Regulate
Transcriptional Signaling and Apoptosis*
,
,**
Department of Pediatrics, University of
California, Los Angeles, California 90095-1752, the
§ University of Texas M. D. Anderson Cancer Center,
Houston, Texas 77030, the ¶ Children's Hospital of Philadelphia,
University of Pennsylvania, Philadelphia, Pennsylvania 19104, and the
Department of Pediatrics, Baylor College of Medicine,
Houston, Texas 77030
(RXR-) as an IGFBP-3 protein partner in a
yeast two-hybrid screen. Multiple methodologies showed that IGFBP-3 and
RXR- bind each other within the nucleus. IGFBP-3-induced apoptosis
was abolished in RXR--knockout cells. IGFBP-3 and RXR ligands were
additive in inducing apoptosis in prostate cancer cells. IGFBP-3
enhanced RXR response element and inhibited RARE signaling. Thus,
RXR--IGFBP-3 interaction leads to modulation of the transcriptional
activity of RXR- and is essential for mediating the effects of
IGFBP-3 on apoptosis.
*
This work was supported in part by Grants 2R01 DK47591 and
1RO1 AI40203 from the National Institutes of Health and by awards from
the Department of Defense, the American Cancer Society, and the
Juvenile Diabetes Foundations (to P. C.). A preliminary account of
this work was presented in part at the Annual Meeting of the Endocrine
Society June 22, 1999, San Diego, CA.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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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