scholarly journals Acute depletion of plasma membrane phosphatidylinositol 4,5-bisphosphate impairs specific steps in endocytosis of the G-protein-coupled receptor

2012 ◽  
Vol 125 (9) ◽  
pp. 2185-2197 ◽  
Author(s):  
D. J. Toth ◽  
J. T. Toth ◽  
G. Gulyas ◽  
A. Balla ◽  
T. Balla ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Comment on "A G Protein Coupled Receptor Is a Plasma Membrane Receptor for the Plant Hormone Abscisic Acid"

Science ◽  
2007 ◽  
Vol 318 (5852) ◽  
pp. 914c-914c ◽  
Author(s):  
C. A. Johnston ◽  
B. R. Temple ◽  
J.-G. Chen ◽  
Y. Gao ◽  
E. N. Moriyama ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Abscisic Acid ◽  
G Protein ◽  
Plant Hormone ◽  
Membrane Receptor ◽  
G Protein Coupled Receptor ◽  
Plasma Membrane Receptor ◽  
G Protein Coupled

scholarly journals Plasma Membrane and Nuclear Localization of G Protein–coupled Receptor Kinase 6A

2007 ◽  
Vol 18 (8) ◽  
pp. 2960-2969 ◽  
Author(s):  
Xiaoshan Jiang ◽  
Jeffrey L. Benovic ◽  
Philip B. Wedegaertner
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
G Protein ◽  
Nuclear Localization ◽  
Nuclear Export ◽  
Amphipathic Helix ◽  
G Protein Coupled Receptor ◽  
C Terminus ◽  
Acidic Residues ◽  
G Protein Coupled

G protein–coupled receptor (GPCR) kinases (GRKs) specifically phosphorylate agonist-occupied GPCRs at the inner surface of the plasma membrane (PM), leading to receptor desensitization. Here we show that the C-terminal 30 amino acids of GRK6A contain multiple elements that either promote or inhibit PM localization. Disruption of palmitoylation by individual mutation of cysteine 561, 562, or 565 or treatment of cells with 2-bromopalmitate shifts GRK6A from the PM to both the cytoplasm and nucleus. Likewise, disruption of the hydrophobic nature of a predicted amphipathic helix by mutation of two leucines to alanines at positions 551 and 552 causes a loss of PM localization. Moreover, acidic amino acids in the C-terminus appear to negatively regulate PM localization; mutational replacement of several acidic residues with neutral or basic residues rescues PM localization of a palmitoylation-defective GRK6A. Last, we characterize the novel nuclear localization, showing that nuclear export of nonpalmitoylated GRK6A is sensitive to leptomycin B and that GRK6A contains a potential nuclear localization signal. Our results suggest that the C-terminus of GRK6A contains a novel electrostatic palmitoyl switch in which acidic residues weaken the membrane-binding strength of the amphipathic helix, thus allowing changes in palmitoylation to regulate PM versus cytoplasmic/nuclear localization.

scholarly journals Activation of the Novel Estrogen Receptor G Protein-Coupled Receptor 30 (GPR30) at the Plasma Membrane

Endocrinology ◽  
2007 ◽  
Vol 148 (7) ◽  
pp. 3236-3245 ◽  
Author(s):  
E. Filardo ◽  
J. Quinn ◽  
Y. Pang ◽  
C. Graeber ◽  
S. Shaw ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
G Protein ◽  
Intracellular Camp ◽  
Calcium Stores ◽  
G Protein Coupled Receptor ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells ◽  
G Protein Coupled

G protein-coupled receptor 30 (GPR30), a seven-transmembrane receptor (7TMR), is associated with rapid estrogen-dependent, G protein signaling and specific estrogen binding. At present, the subcellular site of GPR30 action is unclear. Previous studies using antibodies and fluorochrome-labeled estradiol (E2) have failed to detect GPR30 on the cell surface, suggesting that GPR30 may function uniquely among 7TMRs as an intracellular receptor. Here, we show that detectable expression of GPR30 on the surface of transfected HEK-293 cells can be selected by fluorescence-activated cell sorting. Expression of GPR30 on the cell surface was confirmed by confocal microscopy using the lectin concanavalin A as a plasma membrane marker. Stimulation of GPR30-expressing HEK-293 cells with 17β-E2 caused sequestration of GPR30 from the cell surface and resulted in its codistribution with clathrin and mobilization of intracellular calcium stores. Evidence that GPR30 signals from the cell surface was obtained from experiments demonstrating that the cell-impermeable E2-protein conjugates E2-BSA and E2-horseradish peroxidase promote GPR30-dependent elevation of intracellular cAMP concentrations. Subcellular fractionation studies further support the plasma membrane as a site of GPR30 action with specific [3H]17β-E2 binding and G protein activation associated with plasma membrane but not microsomal, or other fractions, prepared from HEK-293 or SKBR3 breast cancer cells. These results suggest that GPR30, like other 7TMRs, functions as a plasma membrane receptor.

scholarly journals The yeast Ste2p G protein-coupled receptor dimerizes on the cell plasma membrane

2017 ◽  
Vol 1859 (5) ◽  
pp. 698-711 ◽  
Author(s):  
Orkun Cevheroğlu ◽  
Gözde Kumaş ◽  
Melinda Hauser ◽  
Jeffrey M. Becker ◽  
Çağdaş D. Son
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
Cell Plasma Membrane ◽  
Cell Plasma ◽  
G Protein Coupled

scholarly journals Regulation of G Protein-coupled Receptor Trafficking by Inefficient Plasma Membrane Expression

2006 ◽  
Vol 281 (13) ◽  
pp. 8417-8425 ◽  
Author(s):  
Jo Ann Janovick ◽  
Paul E. Knollman ◽  
Shaun P. Brothers ◽  
Rodrigo Ayala-Yáñez ◽  
Abeer S. Aziz ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
Receptor Trafficking ◽  
G Protein Coupled Receptor ◽  
Membrane Expression ◽  
Plasma Membrane Expression ◽  
G Protein Coupled

scholarly journals Segregation of Family A G Protein–Coupled Receptor Protomers in the Plasma Membrane

2013 ◽  
Vol 84 (3) ◽  
pp. 346-352 ◽  
Author(s):  
Anthony Gavalas ◽  
Tien-Hung Lan ◽  
Qiuju Liu ◽  
Ivan R. Corrêa ◽  
Jonathan A. Javitch ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled
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