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
Copyright policy )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
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.
- University of Iowa United States
Sequence Homology, Amino Acid, Amino Acid Motifs, Cell Membrane, Molecular Sequence Data, Neuropeptides, Receptors, LH, Chorionic Gonadotropin, Endocytosis, Two-Hybrid System Techniques, Humans, Amino Acid Sequence, Carrier Proteins, Adaptor Proteins, Signal Transducing, DNA Primers
Sequence Homology, Amino Acid, Amino Acid Motifs, Cell Membrane, Molecular Sequence Data, Neuropeptides, Receptors, LH, Chorionic Gonadotropin, Endocytosis, Two-Hybrid System Techniques, Humans, Amino Acid Sequence, Carrier Proteins, Adaptor Proteins, Signal Transducing, DNA Primers
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