Homologous desensitization of adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor.
TLDR
The data suggest that receptor phosphorylation is involved in homologous as well as heterologous forms of desensitization and may provide a unifying mechanism for desensItization of adenylate cyclase-coupled hormone receptors.About:
This article is published in Journal of Biological Chemistry.The article was published on 1985-04-10 and is currently open access. It has received 125 citations till now. The article focuses on the topics: Homologous desensitization & Cyclase activity.read more
Citations
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G protein-coupled receptor kinases.
TL;DR: This review focuses on the regulation of GRK activity by a variety of allosteric and other factors: agonist-stimulated GPCRs, beta gamma subunits of heterotrimeric GTP- binding proteins, phospholipid cofactors, the calcium-binding proteins calmodulin and recoverin, posttranslational isoprenylation and palmitoylation, autophosphorylation, and protein kinase C-mediated GRK phosphorylation.
Journal ArticleDOI
Molecular mechanisms of receptor desensitization using the β -adrenergic receptor-coupled adenylate cyclase system as a model
TL;DR: New insights into the molecular mechanisms underlying desensitization have emerged from the study of the receptors coupled to the ubiquitous second messenger-generating system adenylate cyclase.
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Regulation of transmembrane signaling by receptor phosphorylation
TL;DR: The role of phosphorylation in regulating receptor function dramatically extends the range of regulatory control of this important covalent modification.
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Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor
TL;DR: The existence of this novel cAMP-independent kinase, which preferentially phosphorylates the agonist-occupied form of the beta-adrenergic receptor, suggests a mechanism that may explain the homologous or agonists-specific form of adenylate cyclase desensitization and suggests a general mechanism for regulation of receptor function.
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Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein)
TL;DR: The results suggest the possibility that a protein analogous to retinal arrestin may exist in other tissues and function in concert with beta-adrenergic receptor kinase to regulate the activity of adenylate cyclase-coupled receptors.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Adenylate cyclase-coupled beta-adrenergic receptors: structure and mechanisms of activation and desensitization.
Journal Article
Agonist-induced desensitization of the beta-adrenergic receptor-linked adenylate cyclase.
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Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor
Jeffrey M. Stadel,Ponnal Nambi,Robert G. L. Shorr,Diane F. Sawyer,Marc G. Caron,Robert J. Lefkowitz +5 more
TL;DR: The data show that catecholamine-induced desensitization of adenylate cyclase in turkey erythrocytes correlates with a stable modification of the beta-adrenergic receptor and is associated with agonist-promoted phosphorylation of beta-receptor peptides.
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Agonist-specific refractoriness induced by isoproterenol. Studies with mutant cells.
TL;DR: The S49 mouse lymphoma cell line is used to study the increase and subsequent decrease in cyclic AMP levels (termed refractoriness) following incubation of cells with isoproterenol, and suggests that adenylate cyclase may exert regulatory controls on beta-adrenergic receptors in addition to generation of cyclicAMP.
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Molecular mechanisms of receptor desensitization using the β -adrenergic receptor-coupled adenylate cyclase system as a model
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