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J. Biol. Chem., Vol. 278, Issue 49, 49348-49357, December 5, 2003

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GIPC Binds to the Human Lutropin Receptor (hLHR) through an Unusual PDZ Domain Binding Motif, and It Regulates the Sorting of the Internalized Human Choriogonadotropin and the Density of Cell Surface hLHR^*

Takashi Hirakawa, Colette Galet, Mikiko Kishi, and Mario Ascoli¶

From the Department of Pharmacology, the University of Iowa, Iowa City, Iowa 52242

By using a yeast two-hybrid screen we identified GIPC (GAIP-interacting protein C terminus), a protein with a type I PDZ domain as a novel human lutropin receptor (hLHR) binding partner. Pull-down and immunoprecipitation assays confirmed this interaction and showed that it is dependent on the PDZ domain of GIPC and the C-terminal tetrapeptide of the hLHR. To characterize the functional consequences of the GIPC-hLHR interaction, we used a small interfering RNA against GIPC to generate a clonal cell line that is deficient in GIPC. Studies with this cell line reveal that GIPC is partially responsible for the recycling of the hormone that is internalized by the hLHR and also for maintaining a relatively constant level of hLHR at the cell surface during hormone internalization.

Received for publication, June 20, 2003 , and in revised form, September 22, 2003.

^* This work was supported in part by National Institutes of Health Grant CA 40629 (to M. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported in part by a fellowship from the Lalor Foundation.

Both authors contributed equally to this work.

^¶ To whom correspondence should be addressed: Dept. of Pharmacology, 2-319B BSB, 51 Newton Rd., The Roy J. and Lucille A. Carver College of Medicine, the University of Iowa, Iowa City, IA 52242. Tel.: 319-335-9907; Fax: 319-335-8930; E-mail: mario-ascoli{at}uiowa.edu.

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