scholarly journals The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

2011 ◽  
Vol 108 (6) ◽  
pp. 2534-2539 ◽  
Author(s):  
M. F. Bolliger ◽  
D. C. Martinelli ◽  
T. C. Sudhof
Keyword(s):  
Cell Adhesion ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
G Protein Coupled

Sphingosine-1-phosphate is a ligand for the G protein-coupled receptor EDG-6

Blood ◽  
2000 ◽  
Vol 95 (8) ◽  
pp. 2624-2629 ◽  
Author(s):  
James R. Van Brocklyn ◽  
Markus H. Gräler ◽  
Günter Bernhardt ◽  
John P. Hobson ◽  
Martin Lipp ◽  
...  
Keyword(s):  
G Protein ◽  
Hek293 Cells ◽  
Hematopoietic Tissue ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Extracellular Signal ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor ◽  
High Concentrations ◽  
G Protein Coupled

Abstract EDG-6 is a recently cloned member of the endothelial differentiation gene (EDG) G protein-coupled receptor family that is expressed in lymphoid and hematopoietic tissue and in the lung. Homology of EDG-6 to the known sphingosine-1-phosphate (SPP) receptors EDG-1, EDG-3, and EDG-5 and lysophosphatidic acid (LPA) receptors EDG-2 and EDG-4 suggested that its ligand may be a lysophospholipid or lysosphingolipid. We examined the binding of [32P]SPP to HEK293 cells, transiently transfected with cDNA encoding EDG-6. Binding of [32P]SPP was saturable, demonstrating high affinity (KD = 63 nmol/L). Binding was also specific for SPP, as only unlabeled SPP and sphinganine-1-phosphate, which lacks the trans double bond at the 4 position, potently displaced radiolabeled SPP. LPA did not compete for binding of SPP at any concentration tested, whereas sphingosylphosphorylcholine competed for binding to EDG-6, but only at very high concentrations. In addition, SPP activated extracellular signal-regulated kinase (Erk) in EDG-6 transfected cells in a pertussis toxin-sensitive manner. These results indicate that EDG-6 is a high affinity receptor for SPP, which couples to a Gi/o protein, resulting in the activation of growth-related signaling pathways.

Sphingosine-1-phosphate is a ligand for the G protein-coupled receptor EDG-6

Blood ◽  
2000 ◽  
Vol 95 (8) ◽  
pp. 2624-2629
Author(s):  
James R. Van Brocklyn ◽  
Markus H. Gräler ◽  
Günter Bernhardt ◽  
John P. Hobson ◽  
Martin Lipp ◽  
...  
Keyword(s):  
G Protein ◽  
Hek293 Cells ◽  
Hematopoietic Tissue ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Extracellular Signal ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor ◽  
High Concentrations ◽  
G Protein Coupled

EDG-6 is a recently cloned member of the endothelial differentiation gene (EDG) G protein-coupled receptor family that is expressed in lymphoid and hematopoietic tissue and in the lung. Homology of EDG-6 to the known sphingosine-1-phosphate (SPP) receptors EDG-1, EDG-3, and EDG-5 and lysophosphatidic acid (LPA) receptors EDG-2 and EDG-4 suggested that its ligand may be a lysophospholipid or lysosphingolipid. We examined the binding of [32P]SPP to HEK293 cells, transiently transfected with cDNA encoding EDG-6. Binding of [32P]SPP was saturable, demonstrating high affinity (KD = 63 nmol/L). Binding was also specific for SPP, as only unlabeled SPP and sphinganine-1-phosphate, which lacks the trans double bond at the 4 position, potently displaced radiolabeled SPP. LPA did not compete for binding of SPP at any concentration tested, whereas sphingosylphosphorylcholine competed for binding to EDG-6, but only at very high concentrations. In addition, SPP activated extracellular signal-regulated kinase (Erk) in EDG-6 transfected cells in a pertussis toxin-sensitive manner. These results indicate that EDG-6 is a high affinity receptor for SPP, which couples to a Gi/o protein, resulting in the activation of growth-related signaling pathways.

Molecular basis of G protein-coupled receptor high affinity for gastrin-releasing peptide (GRP)

2003 ◽  
Vol 124 (4) ◽  
pp. A469
Author(s):  
Tomoo Nakagawa ◽  
Jose A. Tapia ◽  
Kenji Tokita ◽  
Samuel Mantey ◽  
Michael Schumann ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptor ◽  
Gastrin Releasing Peptide ◽  
High Affinity ◽  
G Protein Coupled

The adhesion G protein-coupled receptor G2 (ADGRG2/GPR64) constitutively activates SRE and NFκB and is involved in cell adhesion and migration

2015 ◽  
Vol 27 (12) ◽  
pp. 2579-2588 ◽  
Author(s):  
Miriam C. Peeters ◽  
Michiel Fokkelman ◽  
Bob Boogaard ◽  
Kristoffer L. Egerod ◽  
Bob van de Water ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
G Protein Coupled

scholarly journals Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors

2021 ◽  
Vol 22 (22) ◽  
pp. 12481
Author(s):  
Preethi C. Karnam ◽  
Sergey A. Vishnivetskiy ◽  
Vsevolod V. Gurevich
Keyword(s):  
G Protein ◽  
Receptor Binding ◽  
G Protein Coupled Receptors ◽  
Structural Basis ◽  
Preferential Binding ◽  
High Affinity Receptor ◽  
Functional Forms ◽  
Affinity Receptor ◽  
G Protein Coupled ◽  
Receptor Conformation

Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the receptor, including inactive phosphorylated and active unphosphorylated. The selectivity of arrestins suggests that they must have two sensors, which detect receptor-attached phosphates and the active receptor conformation independently. Simultaneous engagement of both sensors enables arrestin transition into a high-affinity receptor-binding state. This transition involves a global conformational rearrangement that brings additional elements of the arrestin molecule, including the middle loop, in contact with a GPCR, thereby stabilizing the complex. Here, we review structural and mutagenesis data that identify these two sensors and additional receptor-binding elements within the arrestin molecule. While most data were obtained with the arrestin-1-rhodopsin pair, the evidence suggests that all arrestins use similar mechanisms to achieve preferential binding to active phosphorylated GPCRs.

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