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Journal articles on the topic 'GPCR'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

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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2

Lin, Hsi-Hsien. "An Alternative Mode of GPCR Transactivation: Activation of GPCRs by Adhesion GPCRs." International Journal of Molecular Sciences 26, no. 2 (2025): 552. https://doi.org/10.3390/ijms26020552.

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G protein-coupled receptors (GPCRs), critical for cellular communication and signaling, represent the largest cell surface protein family and play important roles in numerous pathophysiological processes. Consequently, GPCRs have become a primary focus in drug discovery efforts. Beyond their traditional G protein-dependent signaling pathways, GPCRs are also capable of activating alternative signaling mechanisms, including G protein-independent signaling, biased signaling, and signaling crosstalk. A particularly novel signaling mode employed by these receptors is GPCR transactivation, which ena

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González-Guede, Irene, María López-Ramos, Luis Rodríguez-Rodríguez, Lydia Abasolo, Arkaitz Mucientes, and Benjamín Fernández-Gutiérrez. "Dysregulation of Glypicans and Notum in Osteoarthritis: Plasma Levels, Bone Marrow Mesenchymal Stromal Cells and Osteoblasts." Cells 13, no. 10 (2024): 852. http://dx.doi.org/10.3390/cells13100852.

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In this study of the alterations of Glypicans 1 to 6 (GPCs) and Notum in plasma, bone marrow mesenchymal stromal cells (BM-MSCs) and osteoblasts in Osteoarthritis (OA), the levels of GPCs and Notum in the plasma of 25 patients and 24 healthy subjects were measured. In addition, BM-MSCs from eight OA patients and eight healthy donors were cultured over a period of 21 days using both a culture medium and an osteogenic medium. Protein and gene expression levels of GPCs and Notum were determined using ELISA and qPCR at 0, 7, 14 and 21 days. GPC5 and Notum levels decreased in the plasma of OA patie

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4

Tany, Ryosuke, Yuhei Goto, Yohei Kondo, and Kazuhiro Aoki. "Quantitative live-cell imaging of GPCR downstream signaling dynamics." Biochemical Journal 479, no. 8 (2022): 883–900. http://dx.doi.org/10.1042/bcj20220021.

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G-protein-coupled receptors (GPCRs) play an important role in sensing various extracellular stimuli, such as neurotransmitters, hormones, and tastants, and transducing the input information into the cell. While the human genome encodes more than 800 GPCR genes, only four Gα-proteins (Gαs, Gαi/o, Gαq/11, and Gα12/13) are known to couple with GPCRs. It remains unclear how such divergent GPCR information is translated into the downstream G-protein signaling dynamics. To answer this question, we report a live-cell fluorescence imaging system for monitoring GPCR downstream signaling dynamics. Genet

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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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6

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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Liu, Samuel, Preston J. Anderson, Sudarshan Rajagopal, Robert J. Lefkowitz, and Howard A. Rockman. "G Protein-Coupled Receptors: A Century of Research and Discovery." Circulation Research 135, no. 1 (2024): 174–97. http://dx.doi.org/10.1161/circresaha.124.323067.

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GPCRs (G protein-coupled receptors), also known as 7 transmembrane domain receptors, are the largest receptor family in the human genome, with ≈800 members. GPCRs regulate nearly every aspect of human physiology and disease, thus serving as important drug targets in cardiovascular disease. Sharing a conserved structure comprised of 7 transmembrane α-helices, GPCRs couple to heterotrimeric G-proteins, GPCR kinases, and β-arrestins, promoting downstream signaling through second messengers and other intracellular signaling pathways. GPCR drug development has led to important cardiovascular therap

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8

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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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

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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11

Yan, Huan, Jingling Zhang, Kam-Tong Leung, et al. "An Update of G-Protein-Coupled Receptor Signaling and Its Deregulation in Gastric Carcinogenesis." Cancers 15, no. 3 (2023): 736. http://dx.doi.org/10.3390/cancers15030736.

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G-protein-coupled receptors (GPCRs) belong to a cell surface receptor superfamily responding to a wide range of external signals. The binding of extracellular ligands to GPCRs activates a heterotrimeric G protein and triggers the production of numerous secondary messengers, which transduce the extracellular signals into cellular responses. GPCR signaling is crucial and imperative for maintaining normal tissue homeostasis. High-throughput sequencing analyses revealed the occurrence of the genetic aberrations of GPCRs and G proteins in multiple malignancies. The altered GPCRs/G proteins serve as

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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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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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14

Lazim, Raudah, Donghyuk Suh, Jai Woo Lee, Thi Ngoc Lan Vu, Sanghee Yoon, and Sun Choi. "Structural Characterization of Receptor–Receptor Interactions in the Allosteric Modulation of G Protein-Coupled Receptor (GPCR) Dimers." International Journal of Molecular Sciences 22, no. 6 (2021): 3241. http://dx.doi.org/10.3390/ijms22063241.

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G protein-coupled receptor (GPCR) oligomerization, while contentious, continues to attract the attention of researchers. Numerous experimental investigations have validated the presence of GPCR dimers, and the relevance of dimerization in the effectuation of physiological functions intensifies the attractiveness of this concept as a potential therapeutic target. GPCRs, as a single entity, have been the main source of scrutiny for drug design objectives for multiple diseases such as cancer, inflammation, cardiac, and respiratory diseases. The existence of dimers broadens the research scope of G

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15

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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Rahman, Md Mominur, Md Rezaul Islam, Sadia Afsana Mim, et al. "Insights into the Promising Prospect of G Protein and GPCR-Mediated Signaling in Neuropathophysiology and Its Therapeutic Regulation." Oxidative Medicine and Cellular Longevity 2022 (September 21, 2022): 1–22. http://dx.doi.org/10.1155/2022/8425640.

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G protein-coupled receptors (GPCRs) are intricately involved in the conversion of extracellular feedback to intracellular responses. These specialized receptors possess a crucial role in neurological and psychiatric disorders. Most nonsensory GPCRs are active in almost 90% of complex brain functions. At the time of receptor phosphorylation, a GPCR pathway is essentially activated through a G protein signaling mechanism via a G protein-coupled receptor kinase (GRK). Dopamine, an important neurotransmitter, is primarily involved in the pathophysiology of several CNS disorders; for instance, bipo

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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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18

Wang, Xiaoyan, Ning Sui, Dandan Hu, Ziwei Zhang, and Tiejun Bing. "Abstract 4712: GPCR panel establishment and application in drug discovery." Cancer Research 84, no. 6_Supplement (2024): 4712. http://dx.doi.org/10.1158/1538-7445.am2024-4712.

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Abstract G protein-coupled receptors (GPCRS) are the largest family of membrane proteins of cell surface receptors. It can be activated by various stimuli and play an important role in various physiological and pathological processes such as cell growth, proliferation, differentiation, metabolism, and homeostasis. Abnormal regulation of GPCR is associated with various human diseases, such as metabolic diseases, cardiovascular diseases, and eye diseases. G protein contains three subunits: α, β, and γ, which form a trimer. When extracellular ligands are bound to GPCRs which activate G protein an

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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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PFLEGER, Kevin D. G., and Karin A. EIDNE. "Monitoring the formation of dynamic G-protein-coupled receptor–protein complexes in living cells." Biochemical Journal 385, no. 3 (2005): 625–37. http://dx.doi.org/10.1042/bj20041361.

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GPCRs (G-protein-coupled receptors) play an extremely important role in transducing extracellular signals across the cell membrane with high specificity and sensitivity. They are central to many of the body's endocrine and neurotransmitter pathways, and are consequently a major drug target. It is now clear that GPCRs interact with a range of proteins, including other GPCRs. Identifying and elucidating the function of such interactions will significantly enhance our understanding of cellular function, with the promise of new and improved pharmaceuticals. Biophysical techniques involving resonan

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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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Wakeling, Madeleine N., Douglas J. Roy, Anthony A. Nash, and James P. Stewart. "Characterization of the murine gammaherpesvirus 68 ORF74 product: a novel oncogenic G protein-coupled receptor." Journal of General Virology 82, no. 5 (2001): 1187–97. http://dx.doi.org/10.1099/0022-1317-82-5-1187.

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Murine gammaherpesvirus (MHV-68) is well established as a small animal model for the study of gammaherpesviruses. The MHV-68 genome contains an open reading frame (ORF74) that has significant sequence homology with mammalian G-protein coupled receptors (GPCRs) and the GPCR from the related Kaposi’s sarcoma-associated herpesvirus (KSHV). Here we show that the MHV-68 ORF74 is predicted to encode a GPCR since it has seven potential transmembrane helices and that it has other sequence motifs in common with GPCRs. Of interest is the observation that the sequence around a conserved arginine at the s

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Zheng, Chen, Liana D. Weinstein, Kevin K. Nguyen, Abhijeet Grewal, Eugenia V. Gurevich, and Vsevolod V. Gurevich. "GPCR Binding and JNK3 Activation by Arrestin-3 Have Different Structural Requirements." Cells 12, no. 12 (2023): 1563. http://dx.doi.org/10.3390/cells12121563.

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Arrestins bind active phosphorylated G protein-coupled receptors (GPCRs). Among the four mammalian subtypes, only arrestin-3 facilitates the activation of JNK3 in cells. In available structures, Lys-295 in the lariat loop of arrestin-3 and its homologue Lys-294 in arrestin-2 directly interact with the activator-attached phosphates. We compared the roles of arrestin-3 conformational equilibrium and Lys-295 in GPCR binding and JNK3 activation. Several mutants with enhanced ability to bind GPCRs showed much lower activity towards JNK3, whereas a mutant that does not bind GPCRs was more active. Th

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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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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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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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Zhao, Xiaoning, Adrie Jones, Keith R. Olson та ін. "A Homogeneous Enzyme Fragment Complementation-Based β-Arrestin Translocation Assay for High-Throughput Screening of G-Protein-Coupled Receptors". Journal of Biomolecular Screening 13, № 8 (2008): 737–47. http://dx.doi.org/10.1177/1087057108321531.

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G-protein-coupled receptors (GPCRs) represent one of the largest gene families in the human genome and have long been regarded as valuable targets for small-molecule drugs. The authors describe a new functional assay that directly monitors GPCR activation. It is based on the interaction between β-arrestin and ligand-activated GPCRs and uses enzyme fragment complementation technology. In this format, a GPCR of interest is fused to a small (~4 kDa), optimized α fragment peptide (termed ProLink™) derived from β-galactosidase, and β-arrestin is fused to an N-terminal deletion mutant of β-galactosi

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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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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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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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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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Gupte, Tejas M., Rabia U. Malik, Ruth F. Sommese, Michael Ritt, and Sivaraj Sivaramakrishnan. "Priming GPCR signaling through the synergistic effect of two G proteins." Proceedings of the National Academy of Sciences 114, no. 14 (2017): 3756–61. http://dx.doi.org/10.1073/pnas.1617232114.

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Although individual G-protein–coupled receptors (GPCRs) are known to activate one or more G proteins, the GPCR–G-protein interaction is viewed as a bimolecular event involving the formation of a ternary ligand–GPCR–G-protein complex. Here, we present evidence that individual GPCR–G-protein interactions can reinforce each other to enhance signaling through canonical downstream second messengers, a phenomenon we term “GPCR priming.” Specifically, we find that the presence of noncognate Gq protein enhances cAMP stimulated by two Gs-coupled receptors, β2-adrenergic receptor (β2-AR) and D1 dopamine

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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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Croft, Wayne, Claire Hill, Eilish McCann, et al. "A Physiologically Required G Protein-coupled Receptor (GPCR)-Regulator of G Protein Signaling (RGS) Interaction That Compartmentalizes RGS Activity." Journal of Biological Chemistry 288, no. 38 (2013): 27327–42. http://dx.doi.org/10.1074/jbc.m113.497826.

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G protein-coupled receptors (GPCRs) can interact with regulator of G protein signaling (RGS) proteins. However, the effects of such interactions on signal transduction and their physiological relevance have been largely undetermined. Ligand-bound GPCRs initiate by promoting exchange of GDP for GTP on the Gα subunit of heterotrimeric G proteins. Signaling is terminated by hydrolysis of GTP to GDP through intrinsic GTPase activity of the Gα subunit, a reaction catalyzed by RGS proteins. Using yeast as a tool to study GPCR signaling in isolation, we define an interaction between the cognate GPCR

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He, Jun, Yi Liu, Yang Lei, and Yiyu Zhu. "Targeting the apelin axis: GPCR-directed peptide therapies for cardiovascular disease." Theoretical and Natural Science 58, no. 1 (2024): 126–31. http://dx.doi.org/10.54254/2753-8818/58/20241355.

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Abstract. G protein-coupled receptors (GPCR)play key roles in various physiological processes, especially in the regulation of cardiovascular function and morphology. The current share of peptide- and protein-antibody-based GPCR drugs is gradually increasing. Several studies have identified and understood the role of GPCR in vasodilatory regulation and cardiac function. In addition, some studies have explored the relationship between GPCRs and CVD-related physiological processes such as inflammation, thrombosis and vascular endothelial function. There is still a gap in the study of GPCRs in CV

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Agbedanu, P., No author No author, M. Brewer, et al. "Involvement of a putative intercellular signal-recognizing G protein-coupled receptor in the engulfment of Salmonella by the protozoan Tetrahymena." Open Veterinary Journal 5, no. 2 (2013): 69. http://dx.doi.org/10.5455/ovj.2013.v3.i2.p69.

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In an effort to investigate the molecular basis of protozoa engulfment-mediated hypervirulence of Salmonella in cattle, we evaluated protozoan G protein-coupled receptors (GPCRs) as transducers of Salmonella engulfment by the model protozoan Tetrahymena. Our laboratory previously demonstrated that non-pathogenic protozoa (including Tetrahymena) engulf Salmonella and then exacerbate its virulence in cattle, but the mechanistic details of the phenomenon are not fully understood. GPCRs were investigated since these receptors facilitate phagocytosis of particulates by Tetrahymena, and a GPCR appar

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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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Venkatakrishnan, A. J., Anthony K. Ma, Rasmus Fonseca, et al. "Diverse GPCRs exhibit conserved water networks for stabilization and activation." Proceedings of the National Academy of Sciences 116, no. 8 (2019): 3288–93. http://dx.doi.org/10.1073/pnas.1809251116.

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G protein-coupled receptors (GPCRs) have evolved to recognize incredibly diverse extracellular ligands while sharing a common architecture and structurally conserved intracellular signaling partners. It remains unclear how binding of diverse ligands brings about GPCR activation, the common structural change that enables intracellular signaling. Here, we identify highly conserved networks of water-mediated interactions that play a central role in activation. Using atomic-level simulations of diverse GPCRs, we show that most of the water molecules in GPCR crystal structures are highly mobile. Se

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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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Saca, Victoria R., Colin Burdette, and Thomas P. Sakmar. "GPCR Biosensors to Study Conformational Dynamics and Signaling in Drug Discovery." Annual Review of Pharmacology and Toxicology 65, no. 1 (2025): 7–28. https://doi.org/10.1146/annurev-pharmtox-061724-080836.

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G protein–coupled receptors (GPCRs) are a superfamily of transmembrane signal transducers that facilitate the flow of chemical signals across membranes. GPCRs are a desirable class of drug targets, and the activation and deactivation dynamics of these receptors are widely studied. Multidisciplinary approaches for studying GPCRs, such as downstream biochemical signaling assays, cryo-electron microscopy structural determinations, and molecular dynamics simulations, have provided insights concerning conformational dynamics and signaling mechanisms. However, new approaches including biosensors tha

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Rinne, Andreas, and Moritz Bünemann. "Charge Movements and Conformational Changes: Biophysical Properties and Physiology of Voltage-Dependent GPCRs." Biomolecules 14, no. 12 (2024): 1652. https://doi.org/10.3390/biom14121652.

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G protein-coupled receptors (GPCRs) regulate multiple cellular functions and represent important drug targets. More than 20 years ago, it was noted that GPCR activation (agonist binding) and signaling (G protein activation) are dependent on the membrane potential (VM). While it is now proven that many GPCRs display an intrinsic voltage dependence, the molecular mechanisms of how GPCRs sense depolarization of the plasma membrane are less well defined. This review summarizes the current knowledge of voltage-dependent signaling in GPCRs. We describe how voltage dependence was discovered in muscar

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Cheng, Han, Calli M. Lear-Rooney, Lisa Johansen, et al. "Inhibition of Ebola and Marburg Virus Entry by G Protein-Coupled Receptor Antagonists." Journal of Virology 89, no. 19 (2015): 9932–38. http://dx.doi.org/10.1128/jvi.01337-15.

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ABSTRACTFiloviruses, consisting of Ebola virus (EBOV) and Marburg virus (MARV), are among the most lethal infectious threats to mankind. Infections by these viruses can cause severe hemorrhagic fevers in humans and nonhuman primates with high mortality rates. Since there is currently no vaccine or antiviral therapy approved for humans, there is an urgent need to develop prophylactic and therapeutic options for use during filoviral outbreaks and bioterrorist attacks. One of the ideal targets against filoviral infection and diseases is at the entry step, which is mediated by the filoviral glycop

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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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Hou, Tianling, Yuemin Bian, Terence McGuire, and Xiang-Qun Xie. "Integrated Multi-Class Classification and Prediction of GPCR Allosteric Modulators by Machine Learning Intelligence." Biomolecules 11, no. 6 (2021): 870. http://dx.doi.org/10.3390/biom11060870.

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G-protein-coupled receptors (GPCRs) are the largest and most diverse group of cell surface receptors that respond to various extracellular signals. The allosteric modulation of GPCRs has emerged in recent years as a promising approach for developing target-selective therapies. Moreover, the discovery of new GPCR allosteric modulators can greatly benefit the further understanding of GPCR cell signaling mechanisms. It is critical but also challenging to make an accurate distinction of modulators for different GPCR groups in an efficient and effective manner. In this study, we focus on an 11-clas

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Wouters, Vasudevan, Crans, Saini, and Stove. "Luminescence- and Fluorescence-Based Complementation Assays to Screen for GPCR Oligomerization: Current State of the Art." International Journal of Molecular Sciences 20, no. 12 (2019): 2958. http://dx.doi.org/10.3390/ijms20122958.

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G protein-coupled receptors (GPCRs) have the propensity to form homo- and heterodimers. Dysfunction of these dimers has been associated with multiple diseases, e.g., pre-eclampsia, schizophrenia, and depression, among others. Over the past two decades, considerable efforts have been made towards the development of screening assays for studying these GPCR dimer complexes in living cells. As a first step, a robust in vitro assay in an overexpression system is essential to identify and characterize specific GPCR–GPCR interactions, followed by methodologies to demonstrate association at endogenous

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Suteau, Valentine, Mathilde Munier, Rym Ben Boubaker, et al. "Identification of Dysregulated Expression of G Protein Coupled Receptors in Endocrine Tumors by Bioinformatics Analysis: Potential Drug Targets?" Cells 11, no. 4 (2022): 703. http://dx.doi.org/10.3390/cells11040703.

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Background: Many studies link G protein-coupled receptors (GPCRs) to cancer. Some endocrine tumors are unresponsive to standard treatment and/or require long-term and poorly tolerated treatment. This study explored, by bioinformatics analysis, the tumoral profiling of the GPCR transcriptome to identify potential targets in these tumors aiming at drug repurposing. Methods: We explored the GPCR differentially expressed genes (DEGs) from public datasets (Gene Expression Omnibus (GEO) database and The Cancer Genome Atlas (TCGA)). The GEO datasets were available for two medullary thyroid cancers (M

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Kotliar, Ilana B., Annika Bendes, Leo Dahl, et al. "Multiplexed mapping of the interactome of GPCRs with receptor activity–modifying proteins." Science Advances 10, no. 31 (2024). http://dx.doi.org/10.1126/sciadv.ado9959.

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Receptor activity–modifying proteins (RAMPs) form complexes with G protein–coupled receptors (GPCRs) and may regulate their cellular trafficking and pharmacology. RAMP interactions have been identified for about 50 GPCRs, but only a few GPCR-RAMP complexes have been studied in detail. To elucidate a comprehensive GPCR-RAMP interactome, we created a library of 215 dual epitope-tagged (DuET) GPCRs representing all GPCR subfamilies and coexpressed each GPCR with each of the three RAMPs. Screening the GPCR-RAMP pairs with customized multiplexed suspension bead array (SBA) immunoassays, we identifi

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Kim, Hyunbin, In-Yeop Baek, and Jihye Seong. "Genetically encoded fluorescent biosensors for GPCR research." Frontiers in Cell and Developmental Biology 10 (September 29, 2022). http://dx.doi.org/10.3389/fcell.2022.1007893.

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G protein-coupled receptors (GPCRs) regulate a wide range of physiological and pathophysiological cellular processes, thus it is important to understand how GPCRs are activated and function in various cellular contexts. In particular, the activation process of GPCRs is dynamically regulated upon various extracellular stimuli, and emerging evidence suggests the subcellular functions of GPCRs at endosomes and other organelles. Therefore, precise monitoring of the GPCR activation process with high spatiotemporal resolution is required to investigate the underlying molecular mechanisms of GPCR fun

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Dahl, Leo, Ilana B. Kotliar, Annika Bendes, et al. "Multiplexed selectivity screening of anti-GPCR antibodies." Science Advances 9, no. 18 (2023). http://dx.doi.org/10.1126/sciadv.adf9297.

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G protein–coupled receptors (GPCRs) control critical cellular signaling pathways. Therapeutic agents including anti-GPCR antibodies (Abs) are being developed to modulate GPCR function. However, validating the selectivity of anti-GPCR Abs is challenging because of sequence similarities among individual receptors within GPCR subfamilies. To address this challenge, we developed a multiplexed immunoassay to test >400 anti-GPCR Abs from the Human Protein Atlas targeting a customized library of 215 expressed and solubilized GPCRs representing all GPCR subfamilies. We found that ~61% of Abs tested

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Feng, Chenlin, Jasper F. Ooms, Erik H. J. Danen, and Laura H. Heitman. "GPCR‐G protein signalling and its mutational landscape in cancer—Driver or passenger." British Journal of Pharmacology, June 12, 2025. https://doi.org/10.1111/bph.70102.

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G protein‐coupled receptors (GPCRs) play a crucial role in cellular signalling, regulating various physiological processes. Abnormal expression and mutations of GPCRs have been implicated in several types of cancer, influencing tumour initiation, progression and immune response. In this review, we present an overview of recent research on GPCR involvement in cancer and discuss the evidence supporting whether mutations in GPCRs act as cancer driver or passenger. Accumulation of GPCR mutations in some highly conserved structural motifs and the mutually exclusiveness observed between Gi‐coupled G

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