GPR3 IS A CONSTITUTIVELY ACTIVE CELL SURFACE G PROTEIN-COUPLED RECEPTOR THAT MAINTAINS MEIOTIC ARREST OF Xenopus laevis OOCYTES

2007 ◽  
Vol 77 (Suppl_1) ◽  
pp. 201-201
Author(s):  
James Deng ◽  
Stephen Hammes
Keyword(s):  
Cell Surface ◽  
Xenopus Laevis ◽  
G Protein ◽  
Active Cell ◽  
Xenopus Laevis Oocytes ◽  
G Protein Coupled Receptor ◽  
Meiotic Arrest ◽  
G Protein Coupled ◽  
Constitutively Active

scholarly journals The Xenopus laevis Isoform of G Protein-Coupled Receptor 3 (GPR3) Is a Constitutively Active Cell Surface Receptor that Participates in Maintaining Meiotic Arrest in X. laevis Oocytes

2008 ◽  
Vol 22 (8) ◽  
pp. 1853-1865 ◽  
Author(s):  
James Deng ◽  
Stephanie Lang ◽  
Christopher Wylie ◽  
Stephen R. Hammes
Keyword(s):  
Cell Surface ◽  
Xenopus Laevis ◽  
G Protein ◽  
Oocyte Maturation ◽  
Cell Surface Receptor ◽  
Xenopus Laevis Oocytes ◽  
Intracellular Camp ◽  
G Protein Coupled Receptor ◽  
Meiotic Arrest ◽  
G Protein Coupled

Abstract Oocytes are held in meiotic arrest in prophase I until ovulation, when gonadotropins trigger a subpopulation of oocytes to resume meiosis in a process termed “maturation.” Meiotic arrest is maintained through a mechanism whereby constitutive cAMP production exceeds phosphodiesterase-mediated degradation, leading to elevated intracellular cAMP. Studies have implicated a constitutively activated Gαs-coupled receptor, G protein-coupled receptor 3 (GPR3), as one of the molecules responsible for maintaining meiotic arrest in mouse oocytes. Here we characterized the signaling and functional properties of GPR3 using the more amenable model system of Xenopus laevis oocytes. We cloned the X. laevis isoform of GPR3 (XGPR3) from oocytes and showed that overexpressed XGPR3 elevated intraoocyte cAMP, in large part via Gβγ signaling. Overexpressed XGPR3 suppressed steroid-triggered kinase activation and maturation of isolated oocytes, as well as gonadotropin-induced maturation of follicle-enclosed oocytes. In contrast, depletion of XGPR3 using antisense oligodeoxynucleotides reduced intracellular cAMP levels and enhanced steroid- and gonadotropin-mediated oocyte maturation. Interestingly, collagenase treatment of Xenopus oocytes cleaved and inactivated cell surface XGPR3, which enhanced steroid-triggered oocyte maturation and activation of MAPK. In addition, human chorionic gonadotropin-treatment of follicle-enclosed oocytes triggered metalloproteinase-mediated cleavage of XGPR3 at the oocyte cell surface. Together, these results suggest that GPR3 moderates the oocyte response to maturation-promoting signals, and that gonadotropin-mediated activation of metalloproteinases may play a partial role in sensitizing oocytes for maturation by inactivating constitutive GPR3 signaling.

scholarly journals A role for GPRx, a novel GPR3/6/12-related G-protein coupled receptor, in the maintenance of meiotic arrest in Xenopus laevis oocytes

2008 ◽  
Vol 317 (1) ◽  
pp. 380-388 ◽  
Author(s):  
Diana Ríos-Cardona ◽  
Roberto R. Ricardo-González ◽  
Ajay Chawla ◽  
James E. Ferrell
Keyword(s):  
Xenopus Laevis ◽  
G Protein ◽  
Xenopus Laevis Oocytes ◽  
G Protein Coupled Receptor ◽  
Meiotic Arrest ◽  
G Protein Coupled

scholarly journals Identification of a Novel Planarian G-Protein-Coupled Receptor That Responds to Serotonin in Xenopus laevis Oocytes

2009 ◽  
Vol 32 (10) ◽  
pp. 1672-1677 ◽  
Author(s):  
Kaneyasu Nishimura ◽  
Kazuhiro Unemura ◽  
Jun Tsushima ◽  
Yosuke Yamauchi ◽  
Jun Otomo ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
G Protein ◽  
Xenopus Laevis Oocytes ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

Effects of Antidepressants on G Protein–coupled Receptor Signaling and Viability in Xenopus laevis  Oocytes

2003 ◽  
Vol 99 (4) ◽  
pp. 911-917 ◽  
Author(s):  
Danja Strümper ◽  
Marcel E. Durieux ◽  
Barbara Tröster ◽  
Klaus Hahnenkamp ◽  
Cristina Vitan ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
G Protein ◽  
Lysophosphatidic Acid ◽  
Local Anesthetics ◽  
Xenopus Laevis Oocytes ◽  
Receptor Signaling ◽  
G Protein Coupled Receptor ◽  
Prolonged Incubation ◽  
Low Concentrations ◽  
G Protein Coupled

Background Tricyclic antidepressants are structurally related to local anesthetics, suggesting that part of their analgesic action may result from properties shared with local anesthetics. Because local anesthetics block G protein-coupled receptor signaling (which explains, in part, their inflammatory modulating properties), the authors studied whether antidepressants have similar effects. Methods Peak Ca-activated Cl currents induced in Xenopus laevis oocytes by lysophosphatidic acid (10(-4) m) were measured using a voltage clamp. The effects of a 30-, 120-, or 240-min incubation in amitriptyline, nortriptyline, imipramine, or fluoxetine were determined. Results After a 30-min incubation, low concentrations (10(-7)-10(-5) m) of antidepressants had no effect on lysophosphatidic acid-induced currents. After prolonged incubation, only amitriptyline or nortriptyline inhibited lysophosphatidic acid signaling (each to 58% of the control response at 10(-7) m after 240 min). At low concentrations, none of the compounds induced membrane damage (defined as a holding current of > 1 microA, 2% in control cells). Imipramine at 10(-3) m induced damage in 100% of oocytes, and fluoxetine at 10(-4) m induced damage in 71% of oocytes (P < 0.05 vs. control). Amitriptyline and nortriptyline had no effect. Conclusions These findings are in part different from those obtained with local anesthetics and suggest that interference with G protein-coupled signaling might explain, in part, the analgesic properties of some antidepressants. However, use of antidepressants in high concentrations may be associated with cellular toxicity.

scholarly journals GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes.

1993 ◽  
Vol 90 (11) ◽  
pp. 5327-5331 ◽  
Author(s):  
S. M. Strittmatter ◽  
S. C. Cannon ◽  
E. M. Ross ◽  
T. Higashijima ◽  
M. C. Fishman
Keyword(s):  
Xenopus Laevis ◽  
G Protein ◽  
Xenopus Laevis Oocytes ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Genetic Variations in the Human G Protein-coupled Receptor Class C, Group 6, Member A (GPRC6A) Control Cell Surface Expression and Function

2016 ◽  
Vol 292 (4) ◽  
pp. 1524-1534 ◽  
Author(s):  
Stine Jørgensen ◽  
Christian Theil Have ◽  
Christina Rye Underwood ◽  
Lars Dan Johansen ◽  
Petrine Wellendorph ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
Control Cell ◽  
Surface Expression ◽  
Genetic Variations ◽  
Cell Surface Expression ◽  
G Protein Coupled Receptor ◽  
Group 6 ◽  
And Function ◽  
G Protein Coupled

Human herpesvirus KSHV encodes a constitutively active G-protein-coupled receptor linked to cell proliferation

Nature ◽  
1997 ◽  
Vol 385 (6614) ◽  
pp. 347-350 ◽  
Author(s):  
Leandros Arvanitakis ◽  
Elizabeth Geras-Raaka ◽  
Anjali Varma ◽  
Marvin C. Gershengorn ◽  
Ethel Cesarman
Keyword(s):  
Cell Proliferation ◽  
G Protein ◽  
Human Herpesvirus ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Constitutively Active

scholarly journals Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein–coupled receptor kinase–dependent manner

2013 ◽  
Vol 24 (11) ◽  
pp. 1649-1660 ◽  
Author(s):  
Susumu Hara ◽  
Shigeki Arawaka ◽  
Hiroyasu Sato ◽  
Youhei Machiya ◽  
Can Cui ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
Dopamine Transporter ◽  
Surface Expression ◽  
Hek293 Cells ◽  
Cell Surface Expression ◽  
Receptor Kinase ◽  
Wild Type ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

Most α-synuclein (α-syn) deposited in Lewy bodies, the pathological hallmark of Parkinson disease (PD), is phosphorylated at Ser-129. However, the physiological and pathological roles of this modification are unclear. Here we investigate the effects of Ser-129 phosphorylation on dopamine (DA) uptake in dopaminergic SH-SY5Y cells expressing α-syn. Subcellular fractionation of small interfering RNA (siRNA)–treated cells shows that G protein–coupled receptor kinase 3 (GRK3), GRK5, GRK6, and casein kinase 2 (CK2) contribute to Ser-129 phosphorylation of membrane-associated α-syn, whereas cytosolic α-syn is phosphorylated exclusively by CK2. Expression of wild-type α-syn increases DA uptake, and this effect is diminished by introducing the S129A mutation into α-syn. However, wild-type and S129A α-syn equally increase the cell surface expression of dopamine transporter (DAT) in SH-SY5Y cells and nonneuronal HEK293 cells. In addition, siRNA-mediated knockdown of GRK5 or GRK6 significantly attenuates DA uptake without altering DAT cell surface expression, whereas knockdown of CK2 has no effect on uptake. Taken together, our results demonstrate that membrane-associated α-syn enhances DA uptake capacity of DAT by GRKs-mediated Ser-129 phosphorylation, suggesting that α-syn modulates intracellular DA levels with no functional redundancy in Ser-129 phosphorylation between GRKs and CK2.

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