Results 21 to 30 of about 10,836 (202)

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.
Benovic, JL, Strasser, RH, Caron, MG, Lefkowitz, RJ   +3 more
openaire   +2 more sources

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 ...
Garcia-Higuera, Irene, Mayor, Federico
openaire   +2 more sources

The β-Adrenergic Receptor Is a Substrate for the Insulin Receptor Tyrosine Kinase [PDF]

Journal of Biological Chemistry, 1996
G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on beta-adrenergic catecholamine action.
Baltensperger, Kurt, Karoor, Vijaya, Paul, Hyacinth, Ruoho, Arnold E., Czech, Michael P., Malbon, Craig C.   +5 more
openaire   +3 more sources

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 ...
C Y, Chen, S B, Dion, C M, Kim, J L, Benovic   +3 more
openaire   +2 more sources

Structure of the human gene encoding the beta-adrenergic receptor kinase.

Journal of Biological Chemistry, 1994
The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the agonist-occupied forms of the beta 2-adrenergic receptor and related G protein-coupled receptors. beta ARK is one of the best characterized members of a growing family of G protein-coupled receptor kinases.
R B, Penn, J L, Benovic
openaire   +2 more sources

The β-Adrenergic Receptor Kinase (GRK2) Is Regulated by Phospholipids [PDF]

Journal of Biological Chemistry, 1995
The beta-adrenergic receptor kinase (beta ARK) is a member of growing family of G protein coupled receptor kinases (GRKs). beta ARK and other members of the GRK family play a role in the mechanism of agonist-specific desensitization by virtue of their ability to phosphorylate G protein-coupled receptors in an agonist-dependent manner.
J J, Onorato, M E, Gillis, Y, Liu, J L, Benovic, A E, Ruoho   +4 more
openaire   +2 more sources

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, J J, Onorato, J L, Arriza, W C, Stone, M, Lohse, N A, Jenkins, D J, Gilbert, N G, Copeland, M G, Caron, R J, Lefkowitz   +9 more
openaire   +2 more sources

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). [PDF]

Proceedings of the National Academy of Sciences, 1987
The beta-adrenergic receptor kinase is an enzyme, possibly analogous to rhodopsin kinase, that multiply phosphorylates the beta-adrenergic receptor only when it is occupied by stimulatory agonists. Since this kinase may play an important role in mediating the process of homologous, or agonist-specific, desensitization, we investigated the functional ...
Benovic, JL, Kühn, H, Weyand, I, Codina, J, Caron, MG, Lefkowitz, RJ   +5 more
openaire   +2 more sources

Metastasis on pause: How dormant tumor cells stay hidden within the tumor microenvironment and evade immune surveillance

Molecular Oncology, EarlyView.
Dormant cancer cells can hide in distant organs for years, evading treatment and the immune system. This review highlights how signals from the surrounding tissue and immune environment keep these cells inactive or trigger their reawakening. Understanding these mechanisms may help develop therapies to eliminate or control dormant cells and prevent ...
Kanishka Tiwary, Jose Javier Bravo‐Cordero   +1 more
wiley   +1 more source

A beta-adrenergic receptor kinase-like enzyme is involved in olfactory signal termination. [PDF]

Proceedings of the National Academy of Sciences, 1993
We have previously shown that second-messenger-dependent kinases (cAMP-dependent kinase, protein kinase C) in the olfactory system are essential in terminating second-messenger signaling in response to odorants. We now document that subtype 2 of the beta-adrenergic receptor kinase (beta ARK) is also involved in this process.
Schleicher, S, Boekhoff, I, Arriza, J, Lefkowitz, RJ, Breer, H   +4 more
openaire   +2 more sources