Up-Regulation of α1B-Adrenergic Receptors with Defects in G Protein Coupling: Ligand-Induced Protection from Receptor Instability

2003 ◽  
Vol 64 (5) ◽  
pp. 1126-1135 ◽  
Author(s):  
Steven C. Prinster ◽  
Nancy A. Schulte ◽  
Megan R. Collins ◽  
Myron L. Toews
Keyword(s):  
G Protein ◽  
Adrenergic Receptors ◽  
G Protein Coupling ◽  
Protein Coupling

scholarly journals Adenosine A1 receptors heterodimerize with β1- and β2-adrenergic receptors creating novel receptor complexes with altered G protein coupling and signaling

2013 ◽  
Vol 25 (4) ◽  
pp. 736-742 ◽  
Author(s):  
P. Charukeshi Chandrasekera ◽  
Tina C. Wan ◽  
Elizabeth T. Gizewski ◽  
John A. Auchampach ◽  
Robert D. Lasley
Keyword(s):  
G Protein ◽  
Adrenergic Receptors ◽  
G Protein Coupling ◽  
Adenosine A1 Receptors ◽  
Protein Coupling ◽  
Receptor Complexes ◽  
Adenosine A1

Glucocorticoids regulate the amount of G proteins in rat aorta

1990 ◽  
Vol 5 (2) ◽  
pp. 185-188 ◽  
Author(s):  
R. M. Haigh ◽  
C. T. Jones ◽  
G. Milligan
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Adrenergic Receptors ◽  
Molecular Mechanisms ◽  
Rat Aorta ◽  
Β Subunit ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Replacement Treatment ◽  
Protein Alterations

ABSTRACT Glucocorticoids are known to influence cardiovascular sensitivity to catecholamines but the molecular mechanisms are undefined. We recently showed that glucocorticoids control the coupling of adrenergic receptors to G protein. Alterations in the amount of G protein is one mechanism by which receptor-G protein coupling may be controlled. Therefore, we set out to measure the levels of G proteins in aorta from normal, adrenalectomized and dexamethasonetreated adrenalectomized rats. G proteins were measured in plasma membrane preparations by immunoblotting and horseradish peroxidase staining. After adrenalectomy there was a 53% (n = 5) decrease in the density of staining for Gi (ANOVA; P<0.05 compared to controls). Conversely, there was a 210% (n = 5) increase in the density of staining for Gs. The levels of Go and the β-subunit of G proteins were not changed by adrenalectomy. Dexamethasone-replacement treatment after adrenalectomy returned Gi and Gs close to control values. Go remained unaltered compared to controls but was 24% (n=3) less than the adrenalectomized values (ANOVA; P<0.05). The levels of β-subunit after dexamethasone replacement were significantly greater (ANOVA; P<0.05) than both the controls and adrenalectomized values. These results show that glucocorticoids can differentially regulate the amounts of G proteins in rat aorta as in other tissues. This may be an important mechanism by which steroids control receptor-G protein coupling and hence transmembrane signalling pathways in vascular smooth muscle.

scholarly journals Ligand recognition, unconventional activation, and G protein coupling of the prostaglandin E2 receptor EP2 subtype

2021 ◽  
Vol 7 (14) ◽  
pp. eabf1268
Author(s):  
Changxiu Qu ◽  
Chunyou Mao ◽  
Peng Xiao ◽  
Qingya Shen ◽  
Ya-Ni Zhong ◽  
...  
Keyword(s):  
G Protein ◽  
Rational Design ◽  
Receptor Activation ◽  
Prostaglandin E ◽  
Toggle Switch ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Ligand Selectivity ◽  
Activation Mechanisms ◽  
Prostaglandin E2 Receptor

Selective modulation of the heterotrimeric G protein α S subunit–coupled prostaglandin E2 (PGE2) receptor EP2 subtype is a promising therapeutic strategy for osteoporosis, ocular hypertension, neurodegenerative diseases, and cardiovascular disorders. Here, we report the cryo–electron microscopy structure of the EP2-Gs complex with its endogenous agonist PGE2 and two synthesized agonists, taprenepag and evatanepag (CP-533536). These structures revealed distinct features of EP2 within the EP receptor family in terms of its unconventional receptor activation and G protein coupling mechanisms, including activation in the absence of a typical W6.48 “toggle switch” and coupling to Gs via helix 8. Moreover, inspection of the agonist-bound EP2 structures uncovered key motifs governing ligand selectivity. Our study provides important knowledge for agonist recognition and activation mechanisms of EP2 and will facilitate the rational design of drugs targeting the PGE2 signaling system.

Functional Domains of the Mouse β3-Adrenoceptor Associated with Differential G Protein Coupling

2005 ◽  
Vol 315 (3) ◽  
pp. 1354-1361 ◽  
Author(s):  
Masaaki Sato ◽  
Dana S. Hutchinson ◽  
Tore Bengtsson ◽  
Anders Floren ◽  
Ülo Langel ◽  
...  
Keyword(s):  
G Protein ◽  
Functional Domains ◽  
G Protein Coupling ◽  
Protein Coupling

scholarly journals Dynamics of receptor/G protein coupling in living cells

2005 ◽  
Vol 24 (23) ◽  
pp. 4106-4114 ◽  
Author(s):  
Peter Hein ◽  
Monika Frank ◽  
Carsten Hoffmann ◽  
Martin J Lohse ◽  
Moritz Bünemann
Keyword(s):  
G Protein ◽  
Living Cells ◽  
G Protein Coupling ◽  
Protein Coupling

Mutant M1 muscarinic receptors with increased agonist affinity and G protein coupling

Life Sciences ◽  
1999 ◽  
Vol 64 (6-7) ◽  
pp. 563
Author(s):  
W.S. Messer ◽  
X.-P. Huang ◽  
P.I. Nagy ◽  
F.E. Williams ◽  
S.M. Peseckis
Keyword(s):  
G Protein ◽  
Muscarinic Receptors ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Agonist Affinity ◽  
M1 Muscarinic ◽  
M1 Muscarinic Receptors
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