Article
Palmitoylation of the luteinizing hormone/human chorionic gonadotropin receptor regulates receptor interaction with the arrestin-mediated internalization pathway.
European journal of biochemistry - 1 Mar 2001
Munshi U M, Peegel H, Menon K M
Abstract excerpt
The luteinizing hormone/human chorionic gonadotropin receptor (LH/hCGR) undergoes palmitoylation at cysteine residues 621 and 622 located in the carboxyl terminal tail of the receptor. This study examined the biological function of palmitoylation with respect to its effect on receptor internalization. Coexpression of wild-type (WT) or C621/622G mutant receptors with arrestin-2 increased receptor internalization...
Topics
- Arrestin
- Cell Line
- Chorionic Gonadotropin
- Endocytosis
- G-Protein-Coupled Receptor Kinase 4
- Humans
- Inositol Phosphates
- Mutation
- Palmitic Acid
- Phosphorylation
- Protein Binding
- Protein Serine-Threonine Kinases
- Receptors, LH
- Tetradecanoylphorbol Acetate