Results 1 to 10 of about 28,675 (270)

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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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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Rapid desensitization of neonatal rat liver beta-adrenergic receptors. A role for beta-adrenergic receptor kinase. [PDF]

Journal of Clinical Investigation, 1994
Exposure of beta-adrenergic receptors (BAR) to agonists often leads to a rapid loss of receptor responsiveness. The proposed mechanisms of such rapid receptor desensitization include receptor phosphorylation by either cAMP-dependent protein kinase or the specific beta-adrenergic receptor kinase (BARK), leading to functional uncoupling from adenylyl ...
Irene García-Higuera, Federico Mayor
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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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Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation [PDF]

Cellular Signalling, 2016
β2-Adrenergic receptors (β2AR) transactivate epidermal growth factor receptors (EGFR) through formation of a β2AR-EGFR complex that requires activation of Src to mediate signaling. Here, we show that both lipid and protein kinase activities of the bifunctional phosphoinositide 3-kinase (PI3K) enzyme are required for β2AR-stimulated EGFR transactivation.
Lewis J. Watson, Kevin Alexander, Maradumane L. Mohan, Amber L. Bowman, Supachoke Mangmool, Kunhong Xiao, Sathyamangla V. Naga Prasad, Howard A. Rockman   +7 more
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Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors. [PDF]

Proceedings of the National Academy of Sciences, 1989
Homologous (agonist-specific) desensitization of beta-adrenergic receptors (beta ARs) is accompanied by and appears to require phosphorylation of the receptors. We have recently described a novel protein kinase, beta AR kinase, which phosphorylates beta ARs in vitro in an agonist-dependent manner.
Martin J. Lohse, Robert J. Lefkowitz, M G Caron, Jeffrey Benovic   +3 more
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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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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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Association of the regulatory beta-adrenergic receptor kinase with rat liver microsomal membranes.

Journal of Biological Chemistry, 1994
beta-Adrenergic receptor kinase (beta ARK) is a regulatory enzyme involved in the modulation of beta-adrenergic and other G protein-coupled receptors. It has been described that beta ARK is a cytosolic protein that transiently translocates to the plasma membrane in order to specifically phosphorylate agonist-occupied receptors.
Irene García-Higuera, Petronila Penela, Cristina Murga, Gustavo Egea, Pedro Bonay, Jeffrey Benovic, Federico Mayor   +6 more
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Cloning, expression, and chromosomal localization of beta-adrenergic receptor kinase 2. A new member of the receptor kinase family

Journal of Biological Chemistry, 1991
The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the agonist-occupied form of the beta-adrenergic and related G protein-coupled receptors. Structural features of this enzyme have been elucidated recently by the isolation of a cDNA that encodes bovine beta ARK.
J.L. Benovic, James J. Onorato, J.L. Arriza, W. Carl Stone, Martin J. Lohse, N.A. Jenkins, Debra J. Gilbert, Neal G. Copeland, Marc G. Caron, Robert J. Lefkowitz   +9 more
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