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Originally published In Press as doi:10.1074/jbc.M104509200 on July 9, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33419-33427, September 7, 2001
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A PDZ Domain Protein Interacts with the C-terminal Tail of the Insulin-like Growth Factor-1 Receptor but Not with the Insulin Receptor*

Tanja LigensaDagger §, Sonia KraussDagger , Dirk DemuthDagger , Ralf SchumacherDagger , Jacques Camonis, Gabriele Jaques§, and K. Michael WeidnerDagger ||

From the Dagger  Roche Diagnostics GmbH, Pharma Research, Nonnenwald 2, Penzberg 82372, Germany, the  Unite INSERM 248, Institut Curie, 26 rue d'Ulm, Paris F-75248, France, and the § Zentrum für Innere Medizin, Abteilung Hämatologie/Onkologie, Philipps-Universität, Baldinger Strasse, Marburg 35033, Germany

In this study, we report on the isolation of a PDZ domain protein, here designated as IIP-1, insulin-like growth factor-1 (IGF-1) receptor-interacting protein-1, which binds to the IGF-1 receptor, but not to the related insulin receptor, and which is involved in the regulation of cell motility. The interaction between the IGF-1 receptor and IIP-1 as well as a splice variant IIP-1/p26 was demonstrated in the yeast two-hybrid system. Using co-precipitation experiments, we confirmed the interaction in transfected cells as well as in vitro. Analysis of deletion mutants indicates that the PDZ domain of IIP-1 mediates interaction with the C-terminal tail of the IGF-1 receptor (serine-threonine-cysteine). This finding demonstrates that the C terminus of the IGF-1 receptor acts as novel PDZ domain binding site. Immunofluorescence analysis revealed an overlapping localization of IIP-1 and the IGF-1 receptor in the breast cancer cell line MCF-7. A functional connection between IIP-1 and the IGF-1 receptor is further supported by the finding that the level of expression of IIP-1 and the IGF-1 receptor strongly correlates in different normal and cancer cells. Furthermore, overexpression of IIP-1 resulted in an attenuation of migration of MCF-7 cells, which is one of the biological activities mediated by the IGF-1 signaling system.

* 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: Dept. of Molecular Biology, Roche Diagnostics GmbH, Pharma Research, Nonnenwald 2, Penzberg, Germany 82372. Tel.: 49-8856-603661; Fax: 49-8856-603604; E-mail: michael.weidner@roche.com.

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