Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

Amino Acids ◽  
2016 ◽  
Vol 48 (12) ◽  
pp. 2875-2880 ◽  
Author(s):  
Daisuke Asai ◽  
Masaharu Murata ◽  
Riki Toita ◽  
Takahito Kawano ◽  
Hideki Nakashima ◽  
...  
Keyword(s):  
Amino Acid ◽  
G Protein ◽  
Phosphorylation Site ◽  
Amino Acid Residues ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
Peptide Substrates ◽  
G Protein Coupled

Chapter 16. The Complex Role of G Protein-coupled Receptor Kinase 2 (GRK2) in Cell Signalling: Beyond GPCR Desensitization

2011 ◽  
pp. 316-334
Author(s):  
Federico Mayor Jr. ◽  
Petronila Penela ◽  
Catalina Ribas ◽  
Cristina Murga
Keyword(s):  
G Protein ◽  
Cell Signalling ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Gpcr Desensitization

scholarly journals Peptide substrates for G protein-coupled receptor kinase 2

FEBS Letters ◽  
2014 ◽  
Vol 588 (13) ◽  
pp. 2129-2132 ◽  
Author(s):  
Daisuke Asai ◽  
Riki Toita ◽  
Masaharu Murata ◽  
Yoshiki Katayama ◽  
Hideki Nakashima ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
Peptide Substrates ◽  
G Protein Coupled

scholarly journals Role of G protein-coupled receptor kinase 2 in tumoral angiogenesis

2014 ◽  
Vol 1 (4) ◽  
pp. e969166 ◽  
Author(s):  
Verónica Rivas ◽  
Laura Nogués ◽  
Clara Reglero ◽  
Federico Mayor ◽  
Petronila Penela
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Regulation of cellular oxidative stress and apoptosis by G protein-coupled receptor kinase-2; The role of NADPH oxidase 4

2016 ◽  
Vol 28 (3) ◽  
pp. 190-203 ◽  
Author(s):  
Tiju Theccanat ◽  
Jennifer L. Philip ◽  
Abdur M. Razzaque ◽  
Nicholas Ludmer ◽  
Jinju Li ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Nadph Oxidase ◽  
G Protein ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
Nadph Oxidase 4 ◽  
G Protein Coupled

scholarly journals Important role of G protein-coupled receptor kinase 5 in homologous desensitization of the thyrotropin receptor.

1996 ◽  
Vol 71 ◽  
pp. 71
Author(s):  
Yuji Nagayama ◽  
Kunihiko Tanaka ◽  
Kohtaro Taniyama ◽  
Masami Niwa
Keyword(s):  
G Protein ◽  
Thyrotropin Receptor ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Homologous Desensitization

scholarly journals THE ROLE OF G PROTEIN-COUPLED RECEPTOR KINASE 4 IN CARDIOMYOCYTE INJURY AFTER MYOCARDIAL INFARCTION

2019 ◽  
Vol 37 ◽  
pp. e84
Author(s):  
L. Li ◽  
L. Tang ◽  
S. Qu ◽  
D. Yang ◽  
Q. Liao ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
G Protein ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Role of Endothelial G Protein-Coupled Receptor Kinase 2 in Angioedema

Hypertension ◽  
2020 ◽  
Vol 76 (5) ◽  
pp. 1625-1636 ◽  
Author(s):  
Jessica Gambardella ◽  
Daniela Sorriento ◽  
Maria Bova ◽  
Mariarosaria Rusciano ◽  
Stefania Loffredo ◽  
...  
Keyword(s):  
Vascular Permeability ◽  
G Protein ◽  
Molecular Mechanisms ◽  
No Production ◽  
Receptor Kinase ◽  
Severe Phenotype ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

Excessive BK (bradykinin) stimulation is responsible for the exaggerated permeabilization of the endothelium in angioedema. However, the molecular mechanisms underlying these responses have not been investigated. BK receptors are Gq-protein-coupled receptors phosphorylated by GRK2 (G protein-coupled receptor kinase 2) with a hitherto unknown biological and pathophysiological significance. In the present study, we sought to identify the functional role of GRK2 in angioedema through the regulation of BK signaling. We found that the accumulation of cytosolic Ca 2+ in endothelial cells induced by BK was sensitive to GRK2 activity, as it was significantly augmented by inhibiting the kinase. Accordingly, permeabilization and NO production induced by BK were enhanced, as well. In vivo, mice with reduced GRK2 levels in the endothelium (Tie2-CRE/GRK2 fl+/fl − ) exhibited an increased response to BK in terms of vascular permeability and extravasation. Finally, patients with reduced GRK2 levels displayed a severe phenotype of angioedema. Taken together, these findings establish GRK2 as a novel pivotal regulator of BK signaling with an essential role in the pathophysiology of vascular permeability and angioedema.

scholarly journals G Protein-coupled Receptor Kinase 2–mediated Phosphorylation of Ezrin Is Required for G Protein-coupled Receptor–dependent Reorganization of the Actin Cytoskeleton

2005 ◽  
Vol 16 (7) ◽  
pp. 3088-3099 ◽  
Author(s):  
Sarah H. Cant ◽  
Julie A. Pitcher
Keyword(s):  
G Protein ◽  
Phosphorylation Site ◽  
Rho Kinase ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
Glutathione S Transferase ◽  
Membrane Ruffling ◽  
Gpcr Activation ◽  
G Protein Coupled

G protein-coupled receptor kinase 2 (GRK2) phosphorylates and desensitizes activated G protein-coupled receptors (GPCRs). Here, we identify ezrin as a novel non-GPCR substrate of GRK2. GRK2 phosphorylates glutathione S-transferase (GST)-ezrin, but not an ezrin fusion protein lacking threonine 567 (T567), in vitro. These results suggest that T567, the regulatory phosphorylation site responsible for maintaining ezrin in its active conformation, represents the principle site of GRK2-mediated phosphorylation. Two lines of evidence indicate that GRK2-mediated ezrin-radixinmoesin (ERM) phosphorylation serves to link GPCR activation to cytoskeletal reorganization. First, in Hep2 cells muscarinic M1 receptor (M1MR) activation causes membrane ruffling. This ruffling response is ERM dependent and is accompanied by ERM phosphorylation. Inhibition of GRK2, but not rho kinase or protein kinase C, prevents ERM phosphorylation and membrane ruffling. Second, agonist-induced internalization of the β2-adrenergic receptor (β2AR) and M1MR is accompanied by ERM phosphorylation and localization of phosphorylated ERM to receptor-containing endocytic vesicles. The colocalization of internalized β2AR and phosphorylated ERM is not dependent on Na+/H+ exchanger regulatory factor binding to the β2AR. Inhibition of ezrin function impedes β2AR internalization, further linking GPCR activation, GRK activity, and ezrin function. Overall, our results suggest that GRK2 serves not only to attenuate but also to transduce GPCR-mediated signals.

The Role of Gβγ and Domain Interfaces in the Activation of G Protein-Coupled Receptor Kinase 2†

Biochemistry ◽  
2005 ◽  
Vol 44 (18) ◽  
pp. 6958-6970 ◽  
Author(s):  
David T. Lodowski ◽  
Jennifer F. Barnhill ◽  
Robyn M. Pyskadlo ◽  
Rodolfo Ghirlando ◽  
Rachel Sterne-Marr ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Role of G‐protein coupled receptor kinase‐2 (GRK2) in the modulation of renal vascular response in SHR by PPAR

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Zivar Yousefipour ◽  
Adebayo Oyekan ◽  
Mohammad Newaz
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
Vascular Response ◽  
G Protein Coupled Receptor ◽  
Renal Vascular ◽  
G Protein Coupled
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