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Artículos de revistas sobre el tema "Receptores GPCR"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 1 de febrero de 2022

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1

Sánchez-Lemus, Enrique, and José A Arias-Montaño. "Transactivación de receptores con actividad de cinasa de tirosina (RTKs) por receptores acoplados a proteínas G." REVISTA BIOMÉDICA 15, no. 1 (2004): 33–48. http://dx.doi.org/10.32776/revbiomed.v15i1.371.

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Los efectos de los factores de crecimiento y de ciertas hormonas se deben a la activación de receptores con actividad intrínseca de cinasa de tirosina (o RTKs, por receptor tyrosine kinases), cuya estimulación inicia cascadas de señalización intracelular que regulan eventos transcripcionales esenciales para la proliferación y la diferenciación celulares. Entre los efectos debidos a la estimulación de los RTKs, destaca la activación de la familia de cinasas de proteína activadas por mitógeno o MAPKs (mitogen-activated protein kinases). Existen evidencias que indican que la estimulación de al

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2

Vidad, Ashley Ryan, Stephen Macaspac, and Ho Leung Ng. "Locating ligand binding sites in G-protein coupled receptors using combined information from docking and sequence conservation." PeerJ 9 (September 24, 2021): e12219. http://dx.doi.org/10.7717/peerj.12219.

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GPCRs (G-protein coupled receptors) are the largest family of drug targets and share a conserved structure. Binding sites are unknown for many important GPCR ligands due to the difficulties of GPCR recombinant expression, biochemistry, and crystallography. We describe our approach, ConDockSite, for predicting ligand binding sites in class A GPCRs using combined information from surface conservation and docking, starting from crystal structures or homology models. We demonstrate the effectiveness of ConDockSite on crystallized class A GPCRs such as the beta2 adrenergic and A2A adenosine recepto

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3

Luttrell, Louis M., та Robert J. Lefkowitz. "The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals". Journal of Cell Science 115, № 3 (2002): 455–65. http://dx.doi.org/10.1242/jcs.115.3.455.

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β-arrestins are versatile adapter proteins that form complexes with most G-protein-coupled receptors (GPCRs) following agonist binding and phosphorylation of receptors by G-protein-coupled receptor kinases (GRKs). They play a central role in the interrelated processes of homologous desensitization and GPCR sequestration, which lead to the termination of G protein activation. β-arrestin binding to GPCRs both uncouples receptors from heterotrimeric G proteins and targets them to clathrin-coated pits for endocytosis. Recent data suggest that β-arrestins also function as GPCR signal transducers. T

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4

Paradis, Justine S., Stevenson Ly, Élodie Blondel-Tepaz та ін. "Receptor sequestration in response to β-arrestin-2 phosphorylation by ERK1/2 governs steady-state levels of GPCR cell-surface expression". Proceedings of the National Academy of Sciences 112, № 37 (2015): E5160—E5168. http://dx.doi.org/10.1073/pnas.1508836112.

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MAPKs are activated in response to G protein-coupled receptor (GPCR) stimulation and play essential roles in regulating cellular processes downstream of these receptors. However, very little is known about the reciprocal effect of MAPK activation on GPCRs. To investigate possible crosstalk between the MAPK and GPCRs, we assessed the effect of ERK1/2 on the activity of several GPCR family members. We found that ERK1/2 activation leads to a reduction in the steady-state cell-surface expression of many GPCRs because of their intracellular sequestration. This subcellular redistribution resulted in

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5

Chattopadhyay, Amitabha. "GPCRs: Lipid-Dependent Membrane Receptors That Act as Drug Targets." Advances in Biology 2014 (October 2, 2014): 1–12. http://dx.doi.org/10.1155/2014/143023.

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G protein-coupled receptors (GPCRs) are the largest class of molecules involved in signal transduction across cell membranes and represent major targets in the development of novel drug candidates in all clinical areas. Although there have been some recent leads, structural information on GPCRs is relatively rare due to the difficulty associated with crystallization. A specific reason for this is the intrinsic flexibility displayed by GPCRs, which is necessary for their functional diversity. Since GPCRs are integral membrane proteins, interaction of membrane lipids with them constitutes an imp

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6

Kapolka, N. J., G. J. Taghon, J. B. Rowe, et al. "DCyFIR: a high-throughput CRISPR platform for multiplexed G protein-coupled receptor profiling and ligand discovery." Proceedings of the National Academy of Sciences 117, no. 23 (2020): 13117–26. http://dx.doi.org/10.1073/pnas.2000430117.

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More than 800 G protein-coupled receptors (GPCRs) comprise the largest class of membrane receptors in humans. While there is ample biological understanding and many approved drugs for prototypic GPCRs, most GPCRs still lack well-defined biological ligands and drugs. Here, we report our efforts to tap the potential of understudied GPCRs by developing yeast-based technologies for high-throughput clustered regularly interspaced short palindromic repeats (CRISPR) engineering and GPCR ligand discovery. We refer to these technologies collectively as Dynamic Cyan Induction by Functional Integrated Re

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7

Lorenzen, Emily, Tea Dodig-Crnković, Ilana B. Kotliar, et al. "Multiplexed analysis of the secretin-like GPCR-RAMP interactome." Science Advances 5, no. 9 (2019): eaaw2778. http://dx.doi.org/10.1126/sciadv.aaw2778.

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Receptor activity–modifying proteins (RAMPs) have been shown to modulate the functions of several G protein–coupled receptors (GPCRs), but potential direct interactions among the three known RAMPs and hundreds of GPCRs have never been investigated. Focusing mainly on the secretin-like family of GPCRs, we engineered epitope-tagged GPCRs and RAMPs, and developed a multiplexed suspension bead array (SBA) immunoassay to detect GPCR-RAMP complexes from detergent-solubilized lysates. Using 64 antibodies raised against the native proteins and 4 antibodies targeting the epitope tags, we mapped the int

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8

Bhattacharya, M., A. V. Babwah, and S. S. G. Ferguson. "Small GTP-binding protein-coupled receptors." Biochemical Society Transactions 32, no. 6 (2004): 1040–44. http://dx.doi.org/10.1042/bst0321040.

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Heterotrimeric GPCRs (G-protein-coupled receptors) form the largest group of integral membrane receptor proteins and mediate diverse physiological processes. In addition to signalling via heterotrimeric G-proteins, GPCRs can also signal by interacting with various small G-proteins to regulate downstream effector pathways. The small G-protein superfamily is structurally classified into at least five families: the Ras, Rho/Rac/cdc42, Rab, Sar1/Arf and Ran families. They are monomeric G-proteins with molecular masses over the range 20–30 kDa, which function as molecular switches to control many e

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9

Southern, Craig, Jennifer M. Cook, Zaynab Neetoo-Isseljee та ін. "Screening β-Arrestin Recruitment for the Identification of Natural Ligands for Orphan G-Protein–Coupled Receptors". Journal of Biomolecular Screening 18, № 5 (2013): 599–609. http://dx.doi.org/10.1177/1087057113475480.

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A variety of G-protein–coupled receptor (GPCR) screening technologies have successfully partnered a number of GPCRs with their cognate ligands. GPCR-mediated β-arrestin recruitment is now recognized as a distinct intracellular signaling pathway, and ligand-receptor interactions may show a bias toward β-arrestin over classical GPCR signaling pathways. We hypothesized that the failure to identify native ligands for the remaining orphan GPCRs may be a consequence of biased β-arrestin signaling. To investigate this, we assembled 10 500 candidate ligands and screened 82 GPCRs using PathHunter β-arr

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10

Sutkeviciute, Ieva, and Jean-Pierre Vilardaga. "Structural insights into emergent signaling modes of G protein–coupled receptors." Journal of Biological Chemistry 295, no. 33 (2020): 11626–42. http://dx.doi.org/10.1074/jbc.rev120.009348.

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G protein–coupled receptors (GPCRs) represent the largest family of cell membrane proteins, with >800 GPCRs in humans alone, and recognize highly diverse ligands, ranging from photons to large protein molecules. Very important to human medicine, GPCRs are targeted by about 35% of prescription drugs. GPCRs are characterized by a seven-transmembrane α-helical structure, transmitting extracellular signals into cells to regulate major physiological processes via heterotrimeric G proteins and β-arrestins. Initially viewed as receptors whose signaling via G proteins is delimited to the plasma mem

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11

Wang, Lei, Lu Zhu, Jaroslawna Meister, et al. "Use of DREADD Technology to Identify Novel Targets for Antidiabetic Drugs." Annual Review of Pharmacology and Toxicology 61, no. 1 (2021): 421–40. http://dx.doi.org/10.1146/annurev-pharmtox-030220-121042.

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G protein–coupled receptors (GPCRs) form a superfamily of plasma membrane receptors that couple to four major families of heterotrimeric G proteins, Gs, Gi, Gq, and G12. GPCRs represent excellent targets for drug therapy. Since the individual GPCRs are expressed by many different cell types, the in vivo metabolic roles of a specific GPCR expressed by a distinct cell type are not well understood. The development of designer GPCRs known as DREADDs (designer receptors exclusively activated by a designer drug) that selectively couple to distinct classes of heterotrimeric G proteins has greatly fac

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12

Kapolka, Nicholas J., Jacob B. Rowe, Geoffrey J. Taghon, William M. Morgan, Corin R. O’Shea, and Daniel G. Isom. "Proton-gated coincidence detection is a common feature of GPCR signaling." Proceedings of the National Academy of Sciences 118, no. 28 (2021): e2100171118. http://dx.doi.org/10.1073/pnas.2100171118.

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The evolutionary expansion of G protein-coupled receptors (GPCRs) has produced a rich diversity of transmembrane sensors for many physical and chemical signals. In humans alone, over 800 GPCRs detect stimuli such as light, hormones, and metabolites to guide cellular decision-making primarily using intracellular G protein signaling networks. This diversity is further enriched by GPCRs that function as molecular sensors capable of discerning multiple inputs to transduce cues encoded in complex, context-dependent signals. Here, we show that many GPCRs are coincidence detectors that couple proton

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13

Tu, Shisheng, Rui Xu, Mengen Wang, Xi Xie, Chenchang Bao, and Dongfa Zhu. "Identification and characterization of expression profiles of neuropeptides and their GPCRs in the swimming crab, Portunus trituberculatus." PeerJ 9 (September 15, 2021): e12179. http://dx.doi.org/10.7717/peerj.12179.

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Neuropeptides and their G protein-coupled receptors (GPCRs) regulate multiple physiological processes. Currently, little is known about the identity of native neuropeptides and their receptors in Portunus trituberculatus. This study employed RNA-sequencing and reverse transcription-polymerase chain reaction (RT-PCR) techniques to identify neuropeptides and their receptors that might be involved in regulation of reproductive processes of P. trituberculatus. In the central nervous system transcriptome data, 47 neuropeptide transcripts were identified. In further analyses, the tissue expression p

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14

Jiang, Yuhong, Xin Zhuo, and Canquan Mao. "G Protein-coupled Receptors in Cancer Stem Cells." Current Pharmaceutical Design 26, no. 17 (2020): 1952–63. http://dx.doi.org/10.2174/1381612826666200305130009.

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G protein-coupled receptors (GPCRs) are highly expressed on a variety of tumour tissues while several GPCR exogenous ligands become marketed pharmaceuticals. In recent decades, cancer stem cells (CSCs) become widely investigated drug targets for cancer therapy but the underlying mechanism is still not fully elucidated. There are vigorous participations of GPCRs in CSCs-related signalling and functions, such as biomarkers for CSCs, activation of Wnt, Hedgehog (HH) and other signalling to facilitate CSCs progressions. This relationship can not only uncover a novel molecular mechanism for GPCR-me

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15

Kruse, Andrew C., Aashish Manglik, Brian K. Kobilka, and William I. Weis. "Applications of molecular replacement to G protein-coupled receptors." Acta Crystallographica Section D Biological Crystallography 69, no. 11 (2013): 2287–92. http://dx.doi.org/10.1107/s090744491301322x.

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G protein-coupled receptors (GPCRs) are a large class of integral membrane proteins involved in regulating virtually every aspect of human physiology. Despite their profound importance in human health and disease, structural information regarding GPCRs has been extremely limited until recently. With the advent of a variety of new biochemical and crystallographic techniques, the structural biology of GPCRs has advanced rapidly, offering key molecular insights into GPCR activation and signal transduction. To date, almost all GPCR structures have been solved using molecular-replacement techniques

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16

Chini, Bice, and Marco Parenti. "G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats." Journal of Molecular Endocrinology 42, no. 5 (2009): 371–79. http://dx.doi.org/10.1677/jme-08-0114.

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G-protein-coupled receptors (GPCRs) are integral membrane proteins, hence it is not surprising that a number of their structural and functional features are modulated by both proteins and lipids. The impact of interacting proteins and lipids on the assembly and signalling of GPCRs has been extensively investigated over the last 20–30 years, and a further impetus has been given by the proposal that GPCRs and/or their immediate signalling partners (G proteins) can partition within plasma membrane domains, termed rafts and caveolae, enriched in glycosphingolipids and cholesterol. The high content

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17

Zheng, Liang-Hong, Chang-He Wang, Shu-Jiang Shang, et al. "Real-time endocytosis imaging as a rapid assay of ligand-GPCR binding in single cells." American Journal of Physiology-Cell Physiology 305, no. 7 (2013): C751—C760. http://dx.doi.org/10.1152/ajpcell.00335.2012.

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Most G protein-coupled receptors (GPCRs) do not generate membrane currents in response to ligand-receptor binding (LRB). Here, we describe a novel technique using endocytosis as a bioassay that can detect activation of a GPCR in a way analogous to patch-clamp recording of an ion channel in a living cell. The confocal imaging technique, termed FM endocytosis imaging (FEI), can record ligand-GPCR binding with high temporal (second) and spatial (micrometer) resolution. LRB leads to internalization of an endocytic vesicle, which can be labeled by a styryl FM dye and visualized as a fluorescent spo

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18

Rivero-Müller, Adolfo, Yen-Yin Chou, Inhae Ji, et al. "Rescue of defective G protein–coupled receptor function in vivo by intermolecular cooperation." Proceedings of the National Academy of Sciences 107, no. 5 (2010): 2319–24. http://dx.doi.org/10.1073/pnas.0906695106.

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G protein–coupled receptors (GPCRs) are ubiquitous mediators of signaling of hormones, neurotransmitters, and sensing. The old dogma is that a one ligand/one receptor complex constitutes the functional unit of GPCR signaling. However, there is mounting evidence that some GPCRs form dimers or oligomers during their biosynthesis, activation, inactivation, and/or internalization. This evidence has been obtained exclusively from cell culture experiments, and proof for the physiological significance of GPCR di/oligomerization in vivo is still missing. Using the mouse luteinizing hormone receptor (L

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19

Rozenfeld, Raphael, and Lakshmi A. Devi. "Exploring a role for heteromerization in GPCR signalling specificity." Biochemical Journal 433, no. 1 (2010): 11–18. http://dx.doi.org/10.1042/bj20100458.

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The critical involvement of GPCRs (G-protein-coupled receptors) in nearly all physiological processes, and the presence of these receptors at the interface between the extracellular and the intracellular milieu, has positioned these receptors as pivotal therapeutic targets. Although a large number of drugs targeting GPCRs are currently available, significant efforts have been directed towards understanding receptor properties, with the goal of identifying and designing improved receptor ligands. Recent advances in GPCR pharmacology have demonstrated that different ligands binding to the same r

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20

Baidya, Mithu, Punita Kumari, Hemlata Dwivedi-Agnihotri та ін. "Genetically encoded intrabody sensors report the interaction and trafficking of β-arrestin 1 upon activation of G-protein–coupled receptors". Journal of Biological Chemistry 295, № 30 (2020): 10153–67. http://dx.doi.org/10.1074/jbc.ra120.013470.

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Agonist stimulation of G-protein–coupled receptors (GPCRs) typically leads to phosphorylation of GPCRs and binding to multifunctional proteins called β-arrestins (βarrs). The GPCR–βarr interaction critically contributes to GPCR desensitization, endocytosis, and downstream signaling, and GPCR–βarr complex formation can be used as a generic readout of GPCR and βarr activation. Although several methods are currently available to monitor GPCR–βarr interactions, additional sensors to visualize them may expand the toolbox and complement existing methods. We have previously described antibody fragmen

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21

Lavington, Steven, and Anthony Watts. "Lipid nanoparticle technologies for the study of G protein-coupled receptors in lipid environments." Biophysical Reviews 12, no. 6 (2020): 1287–302. http://dx.doi.org/10.1007/s12551-020-00775-5.

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AbstractG protein-coupled receptors (GPCRs) are a large family of integral membrane proteins which conduct a wide range of biological roles and represent significant drug targets. Most biophysical and structural studies of GPCRs have been conducted on detergent-solubilised receptors, and it is clear that detergents can have detrimental effects on GPCR function. Simultaneously, there is increasing appreciation of roles for specific lipids in modulation of GPCR function. Lipid nanoparticles such as nanodiscs and styrene maleic acid lipid particles (SMALPs) offer opportunities to study integral m

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22

Weth, Oliver, Simone Haeberlein, Martin Haimann, Yinjie Zhang, and Christoph G. Grevelding. "Towards deorphanizing G protein-coupled receptors of Schistosoma mansoni using the MALAR yeast two-hybrid system." Parasitology 147, no. 8 (2019): 865–72. http://dx.doi.org/10.1017/s0031182019001756.

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AbstractSchistosomiasis is an acute and chronic disease caused by parasitic worms of the genus Schistosoma. Treatment is solely dependent on praziquantel. In the face of the worldwide dimension, projects have been initiated to develop new chemotherapies. Due to their proven druggability, G protein-coupled receptors (GPCRs) are promising targets for anthelmintics. However, to identify candidate receptors, a deeper understanding of GPCR signalling in schistosome biology is essential. Comparative transcriptomics of paired and unpaired worms and their gonads revealed 59 differentially regulated GP

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23

Mishina, Yuji M., Christopher J. Wilson, Linda Bruett, et al. "Multiplex GPCR Assay in Reverse Transfection Cell Microarrays." Journal of Biomolecular Screening 9, no. 3 (2004): 196–207. http://dx.doi.org/10.1177/1087057103261880.

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G protein-coupled receptors (GPCRs) are a superfamily of proteins that include some of the most important drug targets in the pharmaceutical industry. Despite the success of this group of drugs, there remains a need to identify GPCR-targeted drugs with greater selectivity, to develop screening assays for validated targets, and to identify ligands for orphan receptors. To address these challenges, the authors have created a multiplexed GPCR assay that measures greater than 3000 receptor: ligand interactions in a single microplate. The multiplexed assay is generated by combining reverse transfec

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24

Clark, Timothy. "G-Protein coupled receptors: answers from simulations." Beilstein Journal of Organic Chemistry 13 (June 2, 2017): 1071–78. http://dx.doi.org/10.3762/bjoc.13.106.

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Molecular-dynamics (MD) simulations are playing an increasingly important role in research into the modes of action of G-protein coupled receptors (GPCRs). In this field, MD simulations are unusually important as, because of the difficult experimental situation, they often offer the only opportunity to determine structural and mechanistic features in atomistic detail. Modern combinations of soft- and hardware have made MD simulations a powerful tool in GPCR research. This is important because GPCRs are targeted by approximately half of the drugs on the market, so that computer-aided drug desig

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25

HERMANS, Emmanuel, and R. A. John CHALLISS. "Structural, signalling and regulatory properties of the group I metabotropic glutamate receptors: prototypic family C G-protein-coupled receptors." Biochemical Journal 359, no. 3 (2001): 465–84. http://dx.doi.org/10.1042/bj3590465.

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In 1991 a new type of G-protein-coupled receptor (GPCR) was cloned, the type 1a metabotropic glutamate (mGlu) receptor, which, despite possessing the defining seven-transmembrane topology of the GPCR superfamily, bore little resemblance to the growing number of other cloned GPCRs. Subsequent studies have shown that there are eight mammalian mGlu receptors that, together with the calcium-sensing receptor, the GABAB receptor (where GABA is γ-aminobutyric acid) and a subset of pheromone, olfactory and taste receptors, make up GPCR family C. Currently available data suggest that family C GPCRs sha

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Wang, Jialu, Clarice Gareri, and Howard A. Rockman. "G-Protein–Coupled Receptors in Heart Disease." Circulation Research 123, no. 6 (2018): 716–35. http://dx.doi.org/10.1161/circresaha.118.311403.

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GPCRs (G-protein [guanine nucleotide-binding protein]–coupled receptors) play a central physiological role in the regulation of cardiac function in both health and disease and thus represent one of the largest class of surface receptors targeted by drugs. Several antagonists of GPCRs, such as βARs (β-adrenergic receptors) and Ang II (angiotensin II) receptors, are now considered standard of therapy for a wide range of cardiovascular disease, such as hypertension, coronary artery disease, and heart failure. Although the mechanism of action for GPCRs was thought to be largely worked out in the 8

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27

Huang, Jin-Sheng, Lanlan Dong, and Guy C. Le Breton. "Mass-Dependent Cross-Signaling between TXA2 and PAF Receptors." Blood 104, no. 11 (2004): 1557. http://dx.doi.org/10.1182/blood.v104.11.1557.1557.

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Abstract We have previously demonstrated in human platelets that G-protein coupled receptors (GPCRs) which share a common G” subunit have the capacity to cross-signal when exposed to their respective ligands. This ligand-dependent cross-signaling was shown to involve a redistribution of GPCR-coupled G” subunits, a consequent shift in GPCR ligand affinity and a synergistic effector response (Djellas, et al. 1998; PNAS,95:10944 and Djellas, et al. 2000; Biochem.Pharmacol.59:1521). Based on these findings, we proposed that the phenomenon of ligand-dependent cross-signaling represents one manifest

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Ayoub, Mohammed Akli, and Ranjit Vijayan. "Hemorphins Targeting G Protein-Coupled Receptors." Pharmaceuticals 14, no. 3 (2021): 225. http://dx.doi.org/10.3390/ph14030225.

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Hemorphins are short peptides produced by the proteolysis of the beta subunit of hemoglobin. These peptides have diverse physiological effects especially in the nervous and the renin-angiotensin systems. Such effects occur through the modulation of a diverse range of proteins including enzymes and receptors. In this review, we focus on pharmacological and functional targeting of G protein-coupled receptors (GPCRs) by hemorphins and their implication in physiology and pathophysiology. Among GPCRs, the opioid receptors constitute the first set of targets of hemorphins with implication in analges

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N'Diaye, Elsa-Noah, Aylin C. Hanyaloglu, Kimberly K. Kajihara, et al. "The Ubiquitin-like Protein PLIC-2 Is a Negative Regulator of G Protein-coupled Receptor Endocytosis." Molecular Biology of the Cell 19, no. 3 (2008): 1252–60. http://dx.doi.org/10.1091/mbc.e07-08-0775.

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The activity of many signaling receptors is regulated by their endocytosis via clathrin-coated pits (CCPs). For G protein-coupled receptors (GPCRs), recruitment of the adaptor protein arrestin to activated receptors is thought to be sufficient to drive GPCR clustering in CCPs and subsequent endocytosis. We have identified an unprecedented role for the ubiquitin-like protein PLIC-2 as a negative regulator of GPCR endocytosis. Protein Linking IAP to Cytoskeleton (PLIC)-2 overexpression delayed ligand-induced endocytosis of two GPCRs: the V2 vasopressin receptor and β-2 adrenergic receptor, witho

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Barwell, James, Mark Wheatley, Alex C. Conner, et al. "The activation of the CGRP receptor." Biochemical Society Transactions 41, no. 1 (2013): 180–84. http://dx.doi.org/10.1042/bst20120251.

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The CGRP (calcitonin gene-related peptide) receptor is a family B GPCR (G-protein-coupled receptor). It consists of a GPCR, CLR (calcitonin receptor-like receptor) and an accessory protein, RAMP1 (receptor activity modifying protein 1). RAMP1 is needed for CGRP binding and also cell-surface expression of CLR. CLR is an example of a family B GPCR. Unlike family A GPCRs, little is known about how these receptors are activated by their endogenous ligands. This review considers what is known about the activation of family B GPCRs and then considers how this might be applied to CLR, particularly in

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Pellissier, Lucie P., Gaël Barthet, Florence Gaven, et al. "G Protein Activation by Serotonin Type 4 Receptor Dimers." Journal of Biological Chemistry 286, no. 12 (2011): 9985–97. http://dx.doi.org/10.1074/jbc.m110.201939.

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The discovery that class C G protein-coupled receptors (GPCRs) function as obligatory dimeric entities has generated major interest in GPCR oligomerization. Oligomerization now appears to be a common feature among all GPCR classes. However, the functional significance of this process remains unclear because, in vitro, some monomeric GPCRs, such as rhodopsin and β2-adrenergic receptors, activate G proteins. By using wild type and mutant serotonin type 4 receptors (5-HT4Rs) (including a 5-HT4-RASSL) expressed in COS-7 cells as models of class A GPCRs, we show that activation of one protomer in a

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Ellisdon, Andrew M., and Michelle L. Halls. "Compartmentalization of GPCR signalling controls unique cellular responses." Biochemical Society Transactions 44, no. 2 (2016): 562–67. http://dx.doi.org/10.1042/bst20150236.

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With >800 members, G protein-coupled receptors (GPCRs) are the largest class of cell-surface signalling proteins, and their activation mediates diverse physiological processes. GPCRs are ubiquitously distributed across all cell types, involved in many diseases and are major drug targets. However, GPCR drug discovery is still characterized by very high attrition rates. New avenues for GPCR drug discovery may be provided by a recent shift away from the traditional view of signal transduction as a simple chain of events initiated from the plasma membrane. It is now apparent that GPCR signallin

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33

Zhang, Yinjie, Boyang Jason Wu, Xiaolan Yu, et al. "Development of an Antigen-Antibody Co-Display System for Detecting Interaction of G-Protein-Coupled Receptors and Single-Chain Variable Fragments." International Journal of Molecular Sciences 22, no. 9 (2021): 4711. http://dx.doi.org/10.3390/ijms22094711.

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G-protein-coupled receptors (GPCRs), especially chemokine receptors, are ideal targets for monoclonal antibody drugs. Considering the special multi-pass transmembrane structure of GPCR, it is often a laborious job to obtain antibody information about off-targets and epitopes on antigens. To accelerate the process, a rapid and simple method needs to be developed. The split-ubiquitin-based yeast two hybrid system (YTH) was used as a blue script for a new method. By fusing with transmembrane peptides, scFv antibodies were designed to be anchored on the cytomembrane, where the GPCR was co-displaye

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Leifert, Wayne R., Amanda L. Aloia, Olgatina Bucco, Richard V. Glatz, and Edward J. McMurchie. "G-Protein-Coupled Receptors in Drug Discovery: Nanosizing Using Cell-Free Technologies and Molecular Biology Approaches." Journal of Biomolecular Screening 10, no. 8 (2005): 765–79. http://dx.doi.org/10.1177/1087057105280517.

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Signal transduction by G-protein-coupled receptors (GPCRs) underpins a multitude of physiological processes. Ligand recognition by the receptor leads to activation of a genericmolecular switch involving heterotrimeric G-proteins and guanine nucleotides. Signal transduction has been studied extensively with both cell-based systems and assays comprising isolated signaling components. Interest and commercial investment in GPCRs in areas such as drug targets, orphan receptors, highthroughput screening, biosensors, and so on will focus greater attention on assay development to allow for miniaturiza

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Poll, Brian G., Lihe Chen, Chung-Lin Chou, Viswanathan Raghuram, and Mark A. Knepper. "Landscape of GPCR expression along the mouse nephron." American Journal of Physiology-Renal Physiology 321, no. 1 (2021): F50—F68. http://dx.doi.org/10.1152/ajprenal.00077.2021.

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Kidney transport and other renal functions are regulated by multiple G protein-coupled receptors (GPCRs) expressed along the renal tubule. The rapid, recent appearance of comprehensive unbiased gene expression data in the various renal tubule segments, chiefly RNA sequencing and protein mass spectrometry data, has provided a means of identifying patterns of GPCR expression along the renal tubule. To allow for comprehensive mapping, we first curated a comprehensive list of GPCRs in the genomes of mice, rats, and humans ( https://hpcwebapps.cit.nih.gov/ESBL/Database/GPCRs/ ) using multiple onlin

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Zhu, Siyu, Meixian Wu, Ziwei Huang, and Jing An. "Trends in application of advancing computational approaches in GPCR ligand discovery." Experimental Biology and Medicine 246, no. 9 (2021): 1011–24. http://dx.doi.org/10.1177/1535370221993422.

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G protein-coupled receptors (GPCRs) comprise the most important superfamily of protein targets in current ligand discovery and drug development. GPCRs are integral membrane proteins that play key roles in various cellular signaling processes. Therefore, GPCR signaling pathways are closely associated with numerous diseases, including cancer and several neurological, immunological, and hematological disorders. Computer-aided drug design (CADD) can expedite the process of GPCR drug discovery and potentially reduce the actual cost of research and development. Increasing knowledge of biological str

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O'Dowd, Brian F., Mohammad Alijaniaram, Xiaodong Ji, Tuan Nguyen, Richard M. Eglen, and Susan R. George. "Using Ligand-Induced Conformational Change to Screen for Compounds Targeting G-Protein-Coupled Receptors." Journal of Biomolecular Screening 12, no. 2 (2007): 175–85. http://dx.doi.org/10.1177/1087057106298287.

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The authors describe a novel drug strategy designed as a primary screen to discover either antagonist or agonist compounds targeting G-protein-coupled receptors (GPCRs). The incorporation of a nuclear localization sequence (NLS, a 5 amino acid substitution), in a location in helix 8 of the GPCR structure, resulted in ligand-independent receptor translocation from the cell surface to the nucleus. Blockade of the GPCR-NLS translocation from the cell surface was achieved by either antagonist or agonist treatments, each achieving their result in a sensitive concentration-dependent manner. GPCR-NLS

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Ju, Man-Seok, and Sang Taek Jung. "Antigen Design for Successful Isolation of Highly Challenging Therapeutic Anti-GPCR Antibodies." International Journal of Molecular Sciences 21, no. 21 (2020): 8240. http://dx.doi.org/10.3390/ijms21218240.

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G-protein-coupled receptors (GPCR) transmit extracellular signals into cells to regulate a variety of cellular functions and are closely related to the homeostasis of the human body and the progression of various types of diseases. Great attention has been paid to GPCRs as excellent drug targets, and there are many commercially available small-molecule chemical drugs against GPCRs. Despite this, the development of therapeutic anti-GPCR antibodies has been delayed and is challenging due to the difficulty in preparing active forms of GPCR antigens, resulting from their low cellular expression an

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Sato. "Conserved 2nd Residue of Helix 8 of GPCR May Confer the Subclass-Characteristic and Distinct Roles through a Rapid Initial Interaction with Specific G Proteins." International Journal of Molecular Sciences 20, no. 7 (2019): 1752. http://dx.doi.org/10.3390/ijms20071752.

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To obtain a systematic view of the helix-8-second residue responsible for G protein-coupled receptor (GPCR)–G protein initial specific interactions, 786 human GPCRs were subclassified based on the pairs of agonist groups and target G proteins and compared with their conserved second residue of helix 8. Of 314 non-olfactory and deorphanized GPCRs, 273 (87%) conserved single amino acids in the subclasses, while 93 (58%) of the 160 subclasses possessed only a single GPCR member. Class B, C, Frizzled, and trace amine-associated GPCRs demonstrated 100% conservation, whereas class Ⅰ and Ⅱ olfactory

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Kwon, Yong-Jun, Weontae Lee, Auguste Genovesio, and Neil Emans. "A High-Content Subtractive Screen for Selecting Small Molecules Affecting Internalization of GPCRs." Journal of Biomolecular Screening 17, no. 3 (2011): 379–85. http://dx.doi.org/10.1177/1087057111427347.

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G-protein–coupled receptors (GPCRs) are pivotal in cellular responses to the environment and are common drug targets. Identification of selective small molecules acting on single GPCRs is complicated by the shared machinery coupling signal transduction to physiology. Here, we demonstrate a high-content screen using a panel of GPCR assays to identify receptor selective molecules acting within the kinase/phosphatase inhibitor family. A collection of 88 kinase and phosphatase inhibitors was screened against seven agonist-induced GPCR internalization cell models as well as transferrin uptake in hu

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Takahashi, Masaki, Ryo Amano, Michiru Ozawa, Anna Martinez, Kazumasa Akita, and Yoshikazu Nakamura. "Nucleic acid ligands act as a PAM and agonist depending on the intrinsic ligand binding state of P2RY2." Proceedings of the National Academy of Sciences 118, no. 18 (2021): e2019497118. http://dx.doi.org/10.1073/pnas.2019497118.

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G protein–coupled receptors (GPCRs) play diverse roles in physiological processes, and hence the ligands to modulate GPCRs have served as important molecules in biological and pharmacological approaches. However, the exploration of novel ligands for GPCR still remains an arduous challenge. In this study, we report a method for the discovery of nucleic acid ligands against GPCRs by an advanced RNA aptamer screening technology that employs a virus-like particle (VLP), exposing the GPCR of interest. An array of biochemical analyses coupled with a cell-based assay revealed that one of the aptamers

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42

García-Nafría, Javier, and Christopher G. Tate. "Cryo-Electron Microscopy: Moving Beyond X-Ray Crystal Structures for Drug Receptors and Drug Development." Annual Review of Pharmacology and Toxicology 60, no. 1 (2020): 51–71. http://dx.doi.org/10.1146/annurev-pharmtox-010919-023545.

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Electron cryo-microscopy (cryo-EM) has revolutionized structure determination of membrane proteins and holds great potential for structure-based drug discovery. Here we discuss the potential of cryo-EM in the rational design of therapeutics for membrane proteins compared to X-ray crystallography. We also detail recent progress in the field of drug receptors, focusing on cryo-EM of two protein families with established therapeutic value, the γ-aminobutyric acid A receptors (GABAARs) and G protein–coupled receptors (GPCRs). GABAARs are pentameric ion channels, and cryo-EM structures of physiolog

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Wu, Na, Agnieszka M. Olechwier, Cyrill Brunner, et al. "High-mass MALDI-MS unravels ligand-mediated G protein–coupling selectivity to GPCRs." Proceedings of the National Academy of Sciences 118, no. 31 (2021): e2024146118. http://dx.doi.org/10.1073/pnas.2024146118.

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G protein–coupled receptors (GPCRs) are important pharmaceutical targets for the treatment of a broad spectrum of diseases. Although there are structures of GPCRs in their active conformation with bound ligands and G proteins, the detailed molecular interplay between the receptors and their signaling partners remains challenging to decipher. To address this, we developed a high-sensitivity, high-throughput matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) method to interrogate the first stage of signal transduction. GPCR–G protein complex formation is detected as a proxy

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Leysen, Hanne, Jaana van Gastel, Jhana Hendrickx, Paula Santos-Otte, Bronwen Martin, and Stuart Maudsley. "G Protein-Coupled Receptor Systems as Crucial Regulators of DNA Damage Response Processes." International Journal of Molecular Sciences 19, no. 10 (2018): 2919. http://dx.doi.org/10.3390/ijms19102919.

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G protein-coupled receptors (GPCRs) and their associated proteins represent one of the most diverse cellular signaling systems involved in both physiological and pathophysiological processes. Aging represents perhaps the most complex biological process in humans and involves a progressive degradation of systemic integrity and physiological resilience. This is in part mediated by age-related aberrations in energy metabolism, mitochondrial function, protein folding and sorting, inflammatory activity and genomic stability. Indeed, an increased rate of unrepaired DNA damage is considered to be one

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Seo, Sangmin, Jonghwan Choi, Soon Kil Ahn, et al. "Prediction of GPCR-Ligand Binding Using Machine Learning Algorithms." Computational and Mathematical Methods in Medicine 2018 (2018): 1–5. http://dx.doi.org/10.1155/2018/6565241.

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We propose a novel method that predicts binding of G-protein coupled receptors (GPCRs) and ligands. The proposed method uses hub and cycle structures of ligands and amino acid motif sequences of GPCRs, rather than the 3D structure of a receptor or similarity of receptors or ligands. The experimental results show that these new features can be effective in predicting GPCR-ligand binding (average area under the curve [AUC] of 0.944), because they are thought to include hidden properties of good ligand-receptor binding. Using the proposed method, we were able to identify novel ligand-GPCR binding

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46

Thiel, Gerald, Anke Kaufmann, and Oliver G. Rössler. "G-protein-coupled designer receptors – new chemical-genetic tools for signal transduction research." Biological Chemistry 394, no. 12 (2013): 1615–22. http://dx.doi.org/10.1515/hsz-2013-0164.

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Abstract G-protein-coupled receptors (GPCRs) are the largest group of plasma membrane receptors in nature and are activated by a variety of different ligands. The biological outcome of GPCR stimulation is complex, as a plethora of signaling pathways are activated upon stimulation. These complexity and diversity of GPCR signaling make it difficult to manipulate the signaling pathway of a specific GPCR by natural ligands. To reduce the complexity in experimental settings, specific pharmacological ligands that preferentially activate one signaling pathway have been developed. In addition, G-prote

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Akondi, Kalyana Bharati, Marianne Paolini-Bertrand, and Oliver Hartley. "Precision-engineered Peptide and Protein Analogs: Establishing a New Discovery Platform for Potent GPCR Modulators." CHIMIA International Journal for Chemistry 75, no. 6 (2021): 489–94. http://dx.doi.org/10.2533/chimia.2021.489.

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Numerous members of the human G protein-coupled receptor (GPCR) superfamily are receptors of therapeutic interest. GPCRs are considered to be highly tractable for drug discovery, representing the targets of approximately one-third of currently licensed drugs. These successful drug discovery outcomes cover only a relatively small subset of the superfamily, however, and many other attractive receptors have proven to present significant challenges. Among these difficult GPCRs are those whose natural ligands are peptides and proteins. In this review we explain the obstacles faced by GPCR drug disc

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Berger, Miles, David W. Scheel, Hector Macias та ін. "Gαi/o-coupled receptor signaling restricts pancreatic β-cell expansion". Proceedings of the National Academy of Sciences 112, № 9 (2015): 2888–93. http://dx.doi.org/10.1073/pnas.1319378112.

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Gi-GPCRs, G protein-coupled receptors that signal via Gα proteins of the i/o class (Gαi/o), acutely regulate cellular behaviors widely in mammalian tissues, but their impact on the development and growth of these tissues is less clear. For example, Gi-GPCRs acutely regulate insulin release from pancreatic β cells, and variants in genes encoding several Gi-GPCRs—including the α-2a adrenergic receptor, ADRA2A—increase the risk of type 2 diabetes mellitus. However, type 2 diabetes also is associated with reduced total β-cell mass, and the role of Gi-GPCRs in establishing β-cell mass is unknown. T

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49

Ciarkowski, J., P. Drabik, A. Giełdoń, R. Kaźmierkiewicz, and R. Slusarz. "Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination." Acta Biochimica Polonica 48, no. 4 (2001): 1203–7. http://dx.doi.org/10.18388/abp.2001_3892.

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G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the

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50

Guo, Yan-Zhi, Meng-Long Li, Ke-Long Wang, et al. "Fast Fourier Transform-based Support Vector Machine for Prediction of G-protein Coupled Receptor Subfamilies." Acta Biochimica et Biophysica Sinica 37, no. 11 (2005): 759–66. http://dx.doi.org/10.1111/j.1745-7270.2005.00110.x.

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Abstract Although the sequence information on G-protein coupled receptors (GPCRs) continues to grow, many GPCRs remain orphaned (i.e. ligand specificity unknown) or poorly characterized with little structural information available, so an automated and reliable method is badly needed to facilitate the identification of novel receptors. In this study, a method of fast Fourier transform-based support vector machine has been developed for predicting GPCR subfamilies according to protein's hydrophobicity. In classifying Class B, C, D and F subfamilies, the method achieved an overall Matthew's corre

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