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J Biol Chem, Vol. 274, Issue 22, 15745-15750, May 28, 1999

Signal Transduction and Hormone-dependent Internalization of the Thyrotropin-releasing Hormone Receptor in Cells Lacking G_q and G₁₁

From the Department of Pharmacology and Physiology and the Cancer Center, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642

The thyrotropin-releasing hormone (TRH) receptor was expressed in embryonic fibroblasts from mice lacking the  subunits of G_q and G₁₁ (Fq/11 cells) to determine whether G protein coupling is necessary for agonist-dependent receptor internalization. Neither TRH nor agonists acting on endogenous receptors increased intracellular calcium unless the cells were co-transfected with the  subunit of G_q. In contrast, temperature-dependent internalization of [³H]MeTRH in Fq/11 cells was the same whether G_q was expressed or not. A rhodamine-labeled TRH analog and fluorescein-labeled transferrin co-localized in endocytic vesicles in Fq/11 cells, indicating that endocytosis took place via the normal clathrin pathway. Cotransfection with -arrestin or V53D -arrestin increased TRH-dependent receptor sequestration. Fq/11 cells were co-transfected with the TRH receptor and a green fluorescent protein (GFP)--arrestin conjugate. GFP--arrestin was uniformly distributed in the cytoplasm of untreated cells and quickly translocated to the periphery of the cells when TRH was added. A truncated TRH receptor that lacks potential phosphorylation sites in the cytoplasmic carboxyl terminus signaled but did not internalize or cause membrane localization of GFP--arrestin. These results prove that calcium signaling by the TRH receptor requires coupling to a G protein in the G_q family, but TRH-dependent binding of -arrestin and sequestration do not.

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