Molecular and cellular biology of thyrotropin-releasing hormone receptors.
Thyrotropin-releasing hormone (TRH) receptor (TRH-R) complementary DNAs have been cloned from several species. The deduced amino acid sequences are compatible with TRH-R being a seven-transmembrane-spanning G protein-coupled receptor. These complementary DNAs and reagents derived from them have permitted detailed study of TRH-R biology at the molecular and cellular levels. Studies that have been performed since 1990 are reviewed in this article under the following headings: TRH-R gene, tissue distribution of TRH-R, primary structure of TRH-Rs, three-dimensional structure of the TRH-R binding pocket, TRH-R and G proteins, TRH-R activation, TRH desensitization, TRH-R endocytosis, and regulation of TRH-R number. It is evident that many new insights into the structure, function, and regulation of TRH-Rs have been gained in the last several years but that our understanding of these processes is incomplete. We look forward to even greater progress in the future.
Gershengorn
M C
MC
Cornell University Medical College, New York, New York, USA.
Osman
R
R
D000595:Amino Acid Sequence; D000818:Animals; D004705:Endocytosis; D019204:GTP-Binding Proteins / Q000502:physiology; D005796:Genes; D006801:Humans; D008967:Molecular Biology; D008969:Molecular Sequence Data; D018025:Receptors, Thyrotropin-Releasing Hormone / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D014018:Tissue Distribution
D018025:Receptors, Thyrotropin-Releasing Hormone; D019204:GTP-Binding Proteins