Results 1 to 10 of about 10,679 (237)

The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase. [PDF]

Proceedings of the National Academy of Sciences, 1991
Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK.
W Lorenz, James Inglese, Krzysztof Palczewski, James J. Onorato, Marc G. Caron, Robert J. Lefkowitz   +5 more
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Comparative rates of desensitization of beta-adrenergic receptors by the beta-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase. [PDF]

Proceedings of the National Academy of Sciences, 1991
Three separate processes may contribute to rapid beta-adrenergic receptor desensitization: functional uncoupling from the stimulatory guanine nucleotide-binding protein Gs, mediated by phosphorylation of the receptors by two distinct kinases, the specific beta-adrenergic receptor kinase (beta ARK) and the cyclic AMP-dependent protein kinase A (PKA), as
Neil S. Roth, P. Campbell, M G Caron, R.J. Lefkowitz, Martin J. Lohse   +4 more
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Beta-adrenergic receptor kinase. Agonist-dependent receptor binding promotes kinase activation.

Journal of Biological Chemistry, 1993
The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of multiple receptors such as the beta 2-adrenergic receptor (beta 2 AR) and rhodopsin. beta ARK also phosphorylates synthetic peptides, albeit with an approximately 10(4)-10(7)-fold lower Vmax/Km ratio as compared to receptors, with a clear preference for ...
Ching‐Yu Chen, Sarah Dion, C.M. Kim, Jeffrey Benovic   +3 more
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Mechanism of beta-adrenergic receptor kinase activation by G proteins

Journal of Biological Chemistry, 1993
The beta-adrenergic receptor kinase (beta-ARK) specifically phosphorylates the activated form of various G protein-coupled receptors such as the beta 2-adrenergic receptor (beta 2-AR). Recently, G protein beta gamma subunits have been demonstrated to activate beta-ARK-mediated receptor phosphorylation.
C.M. Kim, Sarah Dion, Jeffrey Benovic
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Purification and characterization of the beta-adrenergic receptor kinase.

Journal of Biological Chemistry, 1987
The beta-adrenergic receptor kinase (beta-ARK) is a recently discovered enzyme which specifically phosphorylates the agonist-occupied form of the beta-adrenergic receptor (beta-AR) as well as the light-bleached form of rhodopsin. beta-ARK is present in a wide variety of mammalian tissues.
Jeffrey Benovic, Federico Mayor, C Staniszewski, R J Lefkowitz, Marc G. Caron   +4 more
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Reduced beta-adrenergic receptor activation decreases G-protein expression and beta-adrenergic receptor kinase activity in porcine heart. [PDF]

Journal of Clinical Investigation, 1995
To determine whether beta-adrenergic receptor agonist activation influences guanosine 5'-triphosphate-binding protein (G-protein) expression and beta-adrenergic receptor kinase activity in the heart, we examined the effects of chronic beta 1-adrenergic receptor antagonist treatment (bisoprolol, 0.2 mg/kg per d i.v., 35 d) on components of the ...
Peipei Ping, Ramona Gelzer-Bell, David A. Roth, Douglas P. Kiel, Paul A. Insel, H. Kirk Hammond   +5 more
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Rapid agonist‐induced beta‐adrenergic receptor kinase translocation in C6 glioma cells [PDF]

FEBS Letters, 1992
Exposure of C6 glioma cells to 1 μM isoproterenol leads to fast desensitization of the β‐adrenergic receptor/adenylyl cyclase system and transient receptor sequestration. It also triggers a very rapid and transient translocation to the plasma membrane or β‐adrenergic receptor kinase (βARK), a specific cytoplasmic kinase that phosphorylates only the ...
Irene García-Higuera, Federico Mayor
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Protein kinase translocation following beta-adrenergic receptor activation in C6 glioma cells.

Journal of Biological Chemistry, 1980
Incubation of C6 glioma cells with isoproterenol elicits an increase in cyclic AMP content, followed by an activation of cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37). The cytoplasm of these glioma cells contains type II protein kinase and a small amount of cyclic AMP-independent protein kinase.
Joan P. Schwartz, E. Costa
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Protein kinase cross-talk: membrane targeting of the beta-adrenergic receptor kinase by protein kinase C.

Proceedings of the National Academy of Sciences, 1996
The beta-adrenergic receptor kinase (betaARK) is the prototypical member of the family of cytosolic kinases that phosphorylate guanine nucleotide binding-protein-coupled receptors and thereby trigger uncoupling between receptors and guanine nucleotide binding proteins.
Rainer Winstel, Stefan M.V. Freund, Cornelius Krasel, E. Hoppe, Martin J. Lohse   +4 more
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Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. [PDF]

Proceedings of the National Academy of Sciences, 1986
Agonist-promoted desensitization of adenylate cyclase is intimately associated with phosphorylation of the beta-adrenergic receptor in mammalian, avian, and amphibian cells. However, the nature of the protein kinase(s) involved in receptor phosphorylation remains largely unknown.
Jeffrey Benovic, R. H. Strasser, M G Caron, Robert J. Lefkowitz   +3 more
openalex   +4 more sources