Human β 1- and β 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes

  title={Human $\beta$
 1- and $\beta$
 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes},
  author={Thomas Frielle and Brian K. Kobilka and Robert J. Lefkowitz and Marc G. Caron},
  journal={Trends in Neurosciences},
Bioamine receptors: evolutionary and functional variations of a structural leitmotiv.
The main conformational and functional constraints exerted on the structure of the bioamine receptors are reviewed, mainly the transmembrane conformation of the receptors, their ability to bind ligands, to interact with G-proteins and to desensitize.
Transcription of the rat beta 1-adrenergic receptor gene. Characterization of the transcript and identification of important sequences.
Characterization of the rat beta 1-adrenergic receptor transcript by transient transfection analysis has identified a region between bases -389 and -325 which is necessary for expression and the specific deletion of a potentially functional inverted CCAAT sequence within this region does not significantly alter activity.
Antidepressant-induced Switch of β1-Adrenoceptor Trafficking as a Mechanism for Drug Action*
The data suggest a new mode of drug action causing a “switch” of receptor fate from a fast recycling pathway to a slowly exchanging perinuclear compartment.
Regulation of β1‐Adrenergic Receptor mRNA and Ligand Binding by Antidepressant Treatments and Norepinephrine Depletion in Rat Frontal Cortex
The results demonstrate that β1AR mRNA and ligand binding are regulated in parallel by ECS treatment but that levels of receptor mRNA areregulated in a complex manner by imipramine or 6‐OHDA treatments, not predicted by changes in ligandbinding.
Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor.
  • Y. Tang, L. Hu, R. Lefkowitz
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
The studies demonstrate a role of the SH3p4/p8/p13 protein family in beta1-AR signaling and suggest that interaction between proline-rich motifs and SH3-containing proteins may represent a previously underappreciated aspect of G-protein coupled receptor signaling.
Cloning, Expression of the Human Substance K Receptor, and Analysis of Its Role in Mitogenesis
The human substance K receptor can function as a growth fador receptor when expressed in mouse 3T3 cells and has an apparent molecular weight of 45,000, consistent with little or no N-linked glycosylation.


Ligand binding to the β-adrenergic receptor involves its rhodopsin-like core
The pharmacology of the expressed receptors indicates that most of the hydrophilic residues are not directly involved in the binding of agonists or antagonists to the receptor, and a mutant receptor is identified that has high agonist affinity but does not couple to adenylate cyclase.
Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
Cloning of the gene and cDNA for the mammalian β2AR indicates significant amino-acid homology with bovine rhodopin and suggests that, like rhodopsin7, βAR possesses multiple membrane-spanning regions.
Cloning, sequencing, and expression of the gene coding for the human platelet alpha 2-adrenergic receptor.
The gene for the human platelet alpha 2-adrenergic receptor has been cloned with oligonucleotides corresponding to the partial amino acid sequence of the purified receptor, and two related genes have been identified by low stringency Southern blot analysis.
A comparison of the beta-adrenergic receptor of the turkey erythrocyte with mammalian beta1 and beta2 receptors.
The results demonstrate that the β-adrenergic receptor in the turkey erythrocyte has kinetic and pharmacological properties distinct from either mammalian β1 or β2 receptors.
The mammalian beta 2-adrenergic receptor: purification and characterization.
Peptide mapping and lectin binding studies of the hamster, guinea pig, and rat lung beta 2-adrenergic receptors reveal significant similarities suggestive of evolutionary homology.
Distinct primary structures, ligand‐binding properties and tissue‐specific expression of four human muscarinic acetylcholine receptors.
Differences among subtypes in the affinities and proportions of such sites suggest the capacity of mAChR subtypes to interact differentially with the cellular effector‐coupling apparatus.