scholarly journals Understudied G Protein-Coupled Receptors in the Kidney

Nephron ◽  
2021 ◽  
pp. 1-4
Author(s):  
Nathan A. Zaidman ◽  
Jennifer L. Pluznick
Keyword(s):  
Renal Function ◽  
Cell Surface ◽  
Gene Family ◽  
G Protein ◽  
External Environment ◽  
G Protein Coupled Receptors ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Large Subset ◽  
G Protein Coupled

G protein-coupled receptors (GPCRs) are cell surface proteins which play a key role in allowing cells, tissues, and organs to respond to changes in the external environment in order to maintain homeostasis. Despite the fact that GPCRs are known to play key roles in a variety of tissues, there are a large subset of GPCRs that remain poorly studied. In this minireview, we will summarize what is known regarding the “understudied” GPCRs with respect to renal function, and in so doing will highlight the promise represented by studying this gene family.

scholarly journals ADP-Ribosylation Factors Modulate the Cell Surface Transport of G Protein-Coupled Receptors

2010 ◽  
Vol 333 (1) ◽  
pp. 174-183 ◽  
Author(s):  
Chunmin Dong ◽  
Xiaoping Zhang ◽  
Fuguo Zhou ◽  
Huijuan Dou ◽  
Matthew T. Duvernay ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Surface Transport ◽  
Adp Ribosylation ◽  
G Protein Coupled

The Endoplasmic Reticulum Ca2+-pump SERCA2b Interacts with G Protein-coupled Receptors and Enhances their Expression at the Cell Surface

2007 ◽  
Vol 371 (3) ◽  
pp. 622-638 ◽  
Author(s):  
Jussi T. Tuusa ◽  
Piia M.H. Markkanen ◽  
Pirjo M. Apaja ◽  
Anna E. Hakalahti ◽  
Ulla E. Petäjä-Repo
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Surface ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled

ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors

2006 ◽  
Vol 291 (1) ◽  
pp. C1-C10 ◽  
Author(s):  
Haruhiko Ohtsu ◽  
Peter J. Dempsey ◽  
Satoru Eguchi
Keyword(s):  
G Protein ◽  
Egf Receptor ◽  
Current Knowledge ◽  
G Protein Coupled Receptors ◽  
Surface Proteins ◽  
Egf Receptors ◽  
Cellular Functions ◽  
Egfr Transactivation ◽  
And Migration ◽  
G Protein Coupled

A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as proliferation and migration mediated through multiple G protein-coupled receptors (GPCRs). Recent accumulating evidence has suggested that ADAMs are the key metalloproteases activated by several GPCR agonists to produce a mature EGFR ligand leading to the EGFR transactivation. In this review, we describe the current knowledge on ADAMs implicated in mediating EGFR transactivation. The major focus of the review will be on the possible upstream mechanisms of ADAM activation by GPCRs as well as downstream signal transduction and the pathophysiological significances of ADAM-dependent EGFR transactivation.

Oligomerisation of G-protein-coupled receptors

2001 ◽  
Vol 114 (7) ◽  
pp. 1265-1271 ◽  
Author(s):  
G. Milligan
Keyword(s):  
Energy Transfer ◽  
Cell Surface ◽  
G Protein ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Intact Cells ◽  
Effective Delivery ◽  
Multiple Copies ◽  
Agonist Ligands ◽  
G Protein Coupled

A range of approaches have recently provided evidence that G-protein-coupled receptors can exist as oligomeric complexes. Both homo-oligomers, comprising multiple copies of the same gene product, and hetero-oligomers containing more than one receptor have been detected. In several, but not all, examples, the extent of oligomerisation is regulated by the presence of agonist ligands, and emerging evidence indicates that receptor hetero-oligomers can display distinct pharmacological characteristics. A chaperonin-like role for receptor oligomerisation in effective delivery of newly synthesised receptors to the cell surface is a developing concept, and recent studies have employed a series of energy-transfer techniques to explore the presence and regulation of receptor oligomerisation in living cells. However, the majority of studies have relied largely on co-immunoprecipitation techniques, and there is still little direct information on the fraction of receptors existing as oligomers in intact cells.

scholarly journals Cell-Surface Receptors Transactivation Mediated by G Protein-Coupled Receptors

2014 ◽  
Vol 15 (11) ◽  
pp. 19700-19728 ◽  
Author(s):  
Fabio Cattaneo ◽  
Germano Guerra ◽  
Melania Parisi ◽  
Marta De Marinis ◽  
Domenico Tafuri ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
G Protein Coupled

scholarly journals Structural instability and divergence from conserved residues underlie intracellular retention of mammalian odorant receptors

2020 ◽  
Vol 117 (6) ◽  
pp. 2957-2967
Author(s):  
Kentaro Ikegami ◽  
Claire A. de March ◽  
Maira H. Nagai ◽  
Soumadwip Ghosh ◽  
Matthew Do ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
Surface Expression ◽  
Structural Instability ◽  
G Protein Coupled Receptors ◽  
Machine Learning Techniques ◽  
Odorant Receptors ◽  
Cell Surface Expression ◽  
Conserved Residues ◽  
G Protein Coupled

Mammalian odorant receptors are a diverse and rapidly evolving set of G protein-coupled receptors expressed in olfactory cilia membranes. Most odorant receptors show little to no cell surface expression in nonolfactory cells due to endoplasmic reticulum retention, which has slowed down biochemical studies. Here we provide evidence that structural instability and divergence from conserved residues of individual odorant receptors underlie intracellular retention using a combination of large-scale screening of odorant receptors cell surface expression in heterologous cells, point mutations, structural modeling, and machine learning techniques. We demonstrate the importance of conserved residues by synthesizing consensus odorant receptors that show high levels of cell surface expression similar to conventional G protein-coupled receptors. Furthermore, we associate in silico structural instability with poor cell surface expression using molecular dynamics simulations. We propose an enhanced evolutionary capacitance of olfactory sensory neurons that enable the functional expression of odorant receptors with cryptic mutations.

scholarly journals Title: Single-molecule diffusion-based estimation of ligand effects on G protein-coupled receptors

2017 ◽  
Author(s):  
Masataka Yanagawa ◽  
Michio Hiroshima ◽  
Yuichi Togashi ◽  
Mitsuhiro Abe ◽  
Takahiro Yamashita ◽  
...  
Keyword(s):  
Diffusion Coefficient ◽  
Cell Surface ◽  
G Protein ◽  
Single Molecule ◽  
G Protein Coupled Receptors ◽  
Single Molecule Imaging ◽  
Imaging Analysis ◽  
Coated Pits ◽  
Ligand Effects ◽  
G Protein Coupled

AbstractG protein-coupled receptors (GPCRs) are major drug targets and have high potential for drug discovery. The development of a method for measuring the activities of GPCRs is essential for pharmacology and drug screening. However, it is difficult to measure the effects of a drug by monitoring the receptor on the cell surface, and changes in the concentrations of downstream signaling molecules, which depend on signaling pathway selectivity of the receptor, are used as an index of the receptor activity. Here, we show that single-molecule imaging analysis provides an alternative method for assessing ligand effects on GPCR. We monitored the dynamics of the diffusion of metabotropic glutamate receptor 3 (mGluR3), a class C GPCR, under various ligand conditions by using total internal reflection fluorescence microscopy (TIRFM). The single-molecule tracking analysis demonstrates that changes in the average diffusion coefficient of mGluR3 quantitatively reflect the ligand-dependent activity. Then, we reveal that the diffusion of receptor molecules is altered by the common physiological events associated with GPCRs, including G protein binding or accumulation in clathrin-coated pits, by inhibition experiments and dual-color single-molecule imaging analysis. We also confirm the generality of agonist-induced diffusion change in class A and B GPCRs, demonstrating that the diffusion coefficient is a good index for estimating the ligand effects on many GPCRs regardless of the phylogenetic groups, chemical properties of the ligands, and G protein-coupling selectivity.One Sentence Summary: Single-molecule imaging for evaluating ligand effects on GPCRs by monitoring the diffusion dynamics on the cell surface.

Novel G protein-coupled receptors: a gene family of putative human olfactory receptor sequences

1992 ◽  
Vol 13 (1-2) ◽  
pp. 159-163 ◽  
Author(s):  
Lisa A. Selbie ◽  
Andrea Townsend-Nicholson ◽  
Tiina P. Iismaa ◽  
John Shine
Keyword(s):  
Gene Family ◽  
G Protein ◽  
Olfactory Receptor ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled
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