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Originally published In Press as doi:10.1074/jbc.M005928200 on November 3, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5668-5675, February 23, 2001
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Translation Initiation of the Insulin-like Growth Factor I Receptor mRNA Is Mediated by an Internal Ribosome Entry Site*

Stéphane GiraudDagger , Anna Greco§, Marijke BrinkDagger , Jean-Jacques Diaz§, and Patrick DelafontaineDagger

From the Dagger  Division of Cardiology, University Hospital of Geneva, Rue Micheli-du-Crest 24, 1211 Geneva 14, Switzerland and the § INSERM Unité 369, Faculté de Médecine Lyon RTH Laennec, 7 Rue Guillaume Paradin, 69372 Lyon Cedex 08, France

The insulin-like growth factor I receptor (IGF-IR) is a heterotetrameric receptor mediating the effects of insulin-like growth I and other growth factors. This receptor is encoded by an mRNA containing an unusually long, G-C-rich, and highly structured 5' untranslated region. Using bicistronic constructs, we demonstrated here that the 5' untranslated region of the IGF-IR allows translation initiation by internal ribosome entry and therefore constitutes an internal ribosome entry site. In vitro cross-linking revealed that this internal ribosome entry site binds a protein of 57 kDa. Immunoprecipitation of UV cross-linked proteins proved that this protein was the polypyrimidine tract-binding protein, a well known regulator of picornavirus mRNA translation. The efficiency of translation of the endogenous IGF-IR mRNA is not affected by rapamycin, which is a potent inhibitor of cap-dependent translation. This result provides evidence that the endogenous IGF-IR mRNA is translated, at least in part, through a cap-independent mechanism. This is the first report of a growth factor receptor containing sequence elements that allow translation initiation to occur by internal initiation. Because the IGF-IR has a pivotal function in the cell cycle, this mechanism of translation regulation could play a crucial role in the control of cell proliferation and differentiation.

* This study was supported by NHBLI, National Institutes of Health, Grants HL 47035 and HL 45317, the Swiss Cardiology Foundation, Swiss National Science Foundation Grant FNSR3100-050799.97, and the Gerbex-Bourget Foundation.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.

To whom correspondence should be addressed. Div. of Cardiovascular Diseases, 1001 Eaton Bldg., Kansas University Medical Center, 3901 Rainbow Blvd., Kansas City, KS 66160. Tel.: 913-588-3827; Fax: 913-588-6010; E-mail: PDELAFONTAINE@kumc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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