Identification of G-protein-coupled receptor 120 as a tumor-promoting receptor that induces angiogenesis and migration in human colorectal carcinoma

Oncogene ◽  
2013 ◽  
Vol 32 (49) ◽  
pp. 5541-5550 ◽  
Author(s):  
Q Wu ◽  
H Wang ◽  
X Zhao ◽  
Y Shi ◽  
M Jin ◽  
...  
Keyword(s):  
Colorectal Carcinoma ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
Human Colorectal Carcinoma ◽  
And Migration ◽  
G Protein Coupled

scholarly journals The G Protein-Coupled Receptor Kinases (GRKs) in Chemokine Receptor-Mediated Immune Cell Migration: From Molecular Cues to Physiopathology

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 75
Author(s):  
Marta Laganà ◽  
Géraldine Schlecht-Louf ◽  
Françoise Bachelerie
Keyword(s):  
G Protein ◽  
Chemokine Receptor ◽  
Immune Cell ◽  
Neutrophil Migration ◽  
G Protein Coupled Receptor ◽  
Receptor Kinases ◽  
Immune Cell Migration ◽  
And Migration ◽  
G Protein Coupled ◽  
Gpcr Desensitization

Although G protein-coupled receptor kinases (GRKs) have long been known to regulate G protein-coupled receptor (GPCR) desensitization, their more recently characterized functions as scaffolds and signalling adapters underscore that this small family of proteins governs a larger array of physiological functions than originally suspected. This review explores how GRKs contribute to the complex signalling networks involved in the migration of immune cells along chemokine gradients sensed by cell surface GPCRs. We outline emerging evidence indicating that the coordinated docking of several GRKs on an active chemokine receptor determines a specific receptor phosphorylation barcode that will translate into distinct signalling and migration outcomes. The guidance cues for neutrophil migration are emphasized based on several alterations affecting GRKs or GPCRs reported to be involved in pathological conditions.

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 Adhesion G protein-coupled receptor VLGR1/ADGRV1 regulates cell spreading and migration by mechanosensing at focal adhesions

iScience ◽  
2021 ◽  
Vol 24 (4) ◽  
pp. 102283
Author(s):  
Deva K. Kusuluri ◽  
Baran E. Güler ◽  
Barbara Knapp ◽  
Nicola Horn ◽  
Karsten Boldt ◽  
...  
Keyword(s):  
G Protein ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
G Protein Coupled Receptor ◽  
And Migration ◽  
G Protein Coupled

scholarly journals Arrestins 2 and 3 differentially regulate ETA and P2Y2 receptor-mediated cell signaling and migration in arterial smooth muscle

2012 ◽  
Vol 302 (5) ◽  
pp. C723-C734 ◽  
Author(s):  
Gavin E. Morris ◽  
Carl P. Nelson ◽  
Paul J. Brighton ◽  
Nicholas B. Standen ◽  
R. A. John Challiss ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
G Protein ◽  
Vascular Remodeling ◽  
Vascular Occlusion ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Receptor Desensitization ◽  
G Protein Coupled Receptor ◽  
And Migration ◽  
G Protein Coupled

Overstimulation of endothelin type A (ETA) and nucleotide (P2Y) Gαq-coupled receptors in vascular smooth muscle causes vasoconstriction, hypertension, and, eventually, hypertrophy and vascular occlusion. G protein-coupled receptor kinases (GRKs) and arrestin proteins are sequentially recruited by agonist-occupied Gαq-coupled receptors to terminate phospholipase C signaling, preventing prolonged/inappropriate contractile signaling. However, these proteins also play roles in the regulation of several mitogen-activated protein kinase (MAPK) signaling cascades known to be essential for vascular remodeling. Here we investigated whether different arrestin isoforms regulate endothelin and nucleotide receptor MAPK signaling in rat aortic smooth muscle cells (ASMCs). When intracellular Ca2+ levels were assessed in isolated ASMCs loaded with Ca2+-sensitive dyes, P2Y2 and ETA receptor desensitization was attenuated by selective small-interfering (si)RNA-mediated depletion of G protein-coupled receptor kinase 2 (GRK2). Using similar siRNA techniques, knockdown of arrestin2 prevented P2Y2 receptor desensitization and enhanced and prolonged p38 and ERK MAPK signals, while arrestin3 depletion was ineffective. Conversely, arrestin3 knockdown prevented ETA receptor desensitization and attenuated ET1-stimulated p38 and ERK signals, while arrestin2 depletion had no effect. Using Transwell assays to assess agonist-stimulated ASMC migration, we found that UTP-stimulated migration was markedly attenuated following arrestin2 depletion, while ET1-stimulated migration was attenuated following knockdown of either arrestin. These data highlight a differential arrestin-dependent regulation of ETA and P2Y2 receptor-stimulated MAPK signaling. GRK2 and arrestin expression are essential for agonist-stimulated ASMC migration, which, as a key process in vascular remodeling, highlights the potential roles of GRK2 and arrestin proteins in the progression of vascular disease.

scholarly journals Domain-specific control of germ cell polarity and migration by multifunction Tre1 GPCR

2017 ◽  
Vol 216 (9) ◽  
pp. 2945-2958 ◽  
Author(s):  
Michelle G. LeBlanc ◽  
Ruth Lehmann
Keyword(s):  
Germ Cell ◽  
G Protein ◽  
Primordial Germ Cells ◽  
Cell Polarization ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
G Protein Coupled Receptor ◽  
Single Receptor ◽  
And Migration ◽  
G Protein Coupled

The migration of primordial germ cells (PGCs) from their place of origin to the embryonic gonad is an essential reproductive feature in many animal species. In Drosophila melanogaster, a single G protein–coupled receptor, Trapped in endoderm 1 (Tre1), mediates germ cell polarization at the onset of active migration and directs subsequent migration of PGCs through the midgut primordium. How these different aspects of cell behavior are coordinated through a single receptor is not known. We demonstrate that two highly conserved domains, the E/N/DRY and NPxxY motifs, have overlapping and unique functions in Tre1. The Tre1-NRY domain via G protein signaling is required for reading and responding to guidance and survival cues controlled by the lipid phosphate phosphatases Wunen and Wunen2. In contrast, the Tre1-NPIIY domain has a separate role in Rho1- and E-cadherin–mediated polarization at the initiation stage independent of G protein signaling. We propose that this bifurcation of the Tre1 G protein–coupled receptor signaling response via G protein–dependent and independent branches enables distinct spatiotemporal regulation of germ cell migration.

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