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Journal articles on the topic 'Protein Receptor'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Tibrewal, Richa, Reynoldly Kharsyntiew, Farida Dawood, and Archana Sharma. "A REVIEW ON G-PROTEIN COUPLED RECEPTOR." International Journal of Current Pharmaceutical Review and Research 13, no. 04 (2021): 01–09. https://doi.org/10.5281/zenodo.12664417.

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AbstractG protein–coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domainreceptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linkedreceptors (GPLR), constitute a large protein family of receptors that detect molecules outsidethe cell and activate internal signal transduction pathways and, ultimately, cellular responses.Coupling with G proteins, they are called seven-transmembrane receptors because they passthrough the cell membrane seven times. G protein–coupled receptors are found only ineukaryotes, including yeast, choanof

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Prado, M. A., B. Evans-Bain, and I. M. Dickerson. "Receptor component protein (RCP): a member of a multi-protein complex required for G-protein-coupled signal transduction." Biochemical Society Transactions 30, no. 4 (2002): 460–64. http://dx.doi.org/10.1042/bst0300460.

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The calcitonin-gene-related peptide (CGRP) receptor component protein (RCP) is a 148-amino-acid intracellular protein that is required for G-protein-coupled signal transduction at receptors for the neuropeptide CGRP. RCP works in conjunction with two other proteins to constitute a functional CGRP receptor: calcitonin-receptor-like receptor (CRLR) and receptor-activity-modifying protein 1 (RAMP1).CRLR has the stereotypical seven-transmembrane topology of a G-protein-coupled receptor; it requires RAMP1 for trafficking to the cell surface and for ligand specificity, and requires RCP for coupling

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3

Zeng, Fu-Yue. "Signaling by G Protein-Coupled Receptors." Electronic Journal of Pathology and Histology 6, no. 1 (2000): 13. https://doi.org/10.3233/eph-2000-6_1_13.

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G protein-coupled receptors represent one of the largest families of cell surface receptors in nature. These receptors play fundamental roles in diverse physiological processes such as neurotransmission, cellular metabolism, cell differentiation and growth as well as immune response. In response to extracellular ligands, G protein-coupled receptors specifically interact with heterotrimeric G proteins that can then activate or inhibit effector enzymes, ultimately leading to the physiological response. Biochemical and mutational studies have revealed the molecular mechanisms of ligand-receptor i

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Santiago, Luis, and Ravinder Abrol. "Understanding G Protein Selectivity of Muscarinic Acetylcholine Receptors Using Computational Methods." International Journal of Molecular Sciences 20, no. 21 (2019): 5290. http://dx.doi.org/10.3390/ijms20215290.

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The neurotransmitter molecule acetylcholine is capable of activating five muscarinic acetylcholine receptors, M1 through M5, which belong to the superfamily of G-protein-coupled receptors (GPCRs). These five receptors share high sequence and structure homology; however, the M1, M3, and M5 receptor subtypes signal preferentially through the Gαq/11 subset of G proteins, whereas the M2 and M4 receptor subtypes signal through the Gαi/o subset of G proteins, resulting in very different intracellular signaling cascades and physiological effects. The structural basis for this innate ability of the M1

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Dosil, Mercedes, Kimberly A. Schandel, Ekta Gupta, Duane D. Jenness та James B. Konopka. "The C Terminus of the Saccharomyces cerevisiaeα-Factor Receptor Contributes to the Formation of Preactivation Complexes with Its Cognate G Protein". Molecular and Cellular Biology 20, № 14 (2000): 5321–29. http://dx.doi.org/10.1128/mcb.20.14.5321-5329.2000.

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ABSTRACT Binding of the α-factor pheromone to its G-protein-coupled receptor (encoded by STE2) activates the mating pathway inMATa yeast cells. To investigate whether specific interactions between the receptor and the G protein occur prior to ligand binding, we analyzed dominant-negative mutant receptors that compete with wild-type receptors for G proteins, and we analyzed the ability of receptors to suppress the constitutive signaling activity of mutant Gα subunits in an α-factor-independent manner. Although the amino acid substitution L236H in the third intracellular loop of the receptor imp

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Ferguson, SSG, J. Zhang, LS Barak, and MG Caron. "Pleiotropic Role for GRKs and b-Arrestins in Receptor Regulation." Physiology 12, no. 4 (1997): 145–52. http://dx.doi.org/10.1152/physiologyonline.1997.12.4.145.

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G protein-coupled receptor kinases and arrestin proteins are well-characterized mediators of agonist-dependent G protein-coupled receptor desensitization. These proteins are now shown to play a dual role in receptor regulation by mediating both receptor uncoupling and sequestration, a process important for receptor resensitization. b-Arrestins bound to phosporylated b2-adrenergic and angiotensin II type 1A receptors act as intracellular trafficking molecules specifically targeting these receptors for dynamin-dependent clathrin-coated vesicle-mediated sequestration.

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Brydon, Lena, Florian Roka, Laurence Petit, et al. "Dual Signaling of Human Mel1a Melatonin Receptors via Gi2, Gi3, and Gq/11 Proteins." Molecular Endocrinology 13, no. 12 (1999): 2025–38. http://dx.doi.org/10.1210/mend.13.12.0390.

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Abstract Mel 1a melatonin receptors belong to the superfamily of guanine nucleotide-binding regulatory protein (G protein)-coupled receptors. So far, interest in Mel 1a receptor signaling has focused mainly on the modulation of the adenylyl cyclase pathway via pertussis toxin (PTX)-sensitive G proteins. To further investigate signaling of the human Mel 1a receptor, we have developed an antibody directed against the C terminus of this receptor. This antibody detected the Mel 1a receptor as a protein with an apparent molecular mass of approximately 60 kDa in immunoblots after separation by SDS-P

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8

Oldham, William M., and Heidi E. Hamm. "Structural basis of function in heterotrimeric G proteins." Quarterly Reviews of Biophysics 39, no. 2 (2006): 117–66. http://dx.doi.org/10.1017/s0033583506004306.

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1. Introduction 22. Heterotrimeric G-protein structure 32.1. G-protein α subunit 32.2. G-protein βγ dimer 82.3. Unique role of Gβ5 in complexes with RGS proteins 92.4. Heterotrimer structure 102.5. Lipid modifications direct membrane association 113. Receptor–G protein complex 113.1. Low affinity interactions between inactive receptors (R) and G proteins 113.2. Receptor activation exposes the high-affinity G-protein binding site 123.3. Receptor–G protein interface 143.4. Structural determinants of receptor–G protein specificity 153.5. Models of the receptor–G protein complex 173.6. Sequential

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Milligan, G., H. Murdoch, E. Kellett, J. H. White, and G. J. Feng. "Interactions between G-protein-coupled receptors and periplakin: a selective means to regulate G-protein activation." Biochemical Society Transactions 32, no. 5 (2004): 878–80. http://dx.doi.org/10.1042/bst0320878.

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A substantial number of G-protein-coupled receptor-interacting proteins have been identified initially by the use of yeast two-hybrid screens. Using the C-terminal tail of both opioid receptors and the melanin concentrating hormone receptor-1 as bait, the actin and intermediate filament-binding protein periplakin was isolated. In each case, the site of interaction is within helix VIII of the receptor and periplakin limits agonist-mediated G-protein activation potentially by competing with G-protein for this region of the receptor.

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10

Okashah, Najeah, Shane C. Wright, Kouki Kawakami, et al. "Agonist-induced formation of unproductive receptor-G12complexes." Proceedings of the National Academy of Sciences 117, no. 35 (2020): 21723–30. http://dx.doi.org/10.1073/pnas.2003787117.

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G proteins are activated when they associate with G protein-coupled receptors (GPCRs), often in response to agonist-mediated receptor activation. It is generally thought that agonist-induced receptor-G protein association necessarily promotes G protein activation and, conversely, that activated GPCRs do not interact with G proteins that they do not activate. Here we show that GPCRs can form agonist-dependent complexes with G proteins that they do not activate. Using cell-based bioluminescence resonance energy transfer (BRET) and luminescence assays we find that vasopressin V2receptors (V2R) as

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Fischer, J. A., R. Muff, and W. Born. "Functional relevance of G-protein-coupled-receptor-associated proteins, exemplified by receptor-activity-modifying proteins (RAMPs)." Biochemical Society Transactions 30, no. 4 (2002): 455–60. http://dx.doi.org/10.1042/bst0300455.

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The calcitonin (CT) receptor (CTR) and the CTR-like receptor (CRLR) are close relatives within the type II family of G-protein-coupled receptors, demonstrating sequence identity of 50%. Unlike the interaction between CT and CTR, receptors for the related hormones and neuropeptides amylin, CT-gene-related peptide (CGRP) and adrenomedullin (AM) require one of three accessory receptor-activity-modifying proteins (RAMPs) for ligand recognition. An amylin/CGRP receptor is revealed when CTR is co-expressed with RAMP1. When complexed with RAMP3, CTR interacts with amylin alone. CRLR, initially classe

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Gurevich, Eugenia V., and Vsevolod V. Gurevich. "GRKs as Modulators of Neurotransmitter Receptors." Cells 10, no. 1 (2020): 52. http://dx.doi.org/10.3390/cells10010052.

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Many receptors for neurotransmitters, such as dopamine, norepinephrine, acetylcholine, and neuropeptides, belong to the superfamily of G protein-coupled receptors (GPCRs). A general model posits that GPCRs undergo two-step homologous desensitization: the active receptor is phosphorylated by kinases of the G protein-coupled receptor kinase (GRK) family, whereupon arrestin proteins specifically bind active phosphorylated receptors, shutting down G protein-mediated signaling, facilitating receptor internalization, and initiating distinct signaling pathways via arrestin-based scaffolding. Here, we

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Jänne, O. A., A. M. Moilanen, H. Poukka, et al. "Androgen-receptor-interacting nuclear proteins." Biochemical Society Transactions 28, no. 4 (2000): 401–5. http://dx.doi.org/10.1042/bst0280401.

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Androgen receptor (AR) belongs to the super-family of nuclear hormone receptors that employ complex molecular mechanisms to guide the development and physiological functions of their target tissues. Our recent work has led to the identification of four novel proteins that recognize AR zinc-finger region (ZFR) both in vivo and in vitro. One is a small nuclear RING-finger protein that possesses separate interaction interfaces for AR and for other transcription activators such as Spl. The second is a nuclear serine/threonine protein kinase (androgen-receptor-interacting nuclear protein kinase; AN

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14

Moskalev, Alexander V., Boris Yu Gumilevskiy, Vasiliy Ya Apchel, and Vasiliy N. Cygan. "T-cell receptor family, signal transduction, and transcription factors in T-cell immune response." Bulletin of the Russian Military Medical Academy 27, no. 1 (2025): 135–46. https://doi.org/10.17816/brmma636850.

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This study investigated signal transduction in T-lymphocytes, whose cell receptors are categorized into several groups based on their signaling mechanisms and the intracellular biochemical pathways they activate, including modular signaling proteins and adapter molecules that perform scaffolding or catalytic functions. Adapter proteins facilitate signaling complexes by linking various enzymes. Immune receptors, which are composed of integral membrane proteins from the immunoglobulin superfamily, interact with specific tyrosine-containing motifs within transmembrane signaling proteins in their

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Lu, Sumin, Wonjo Jang, Asuka Inoue, and Nevin A. Lambert. "Constitutive G protein coupling profiles of understudied orphan GPCRs." PLOS ONE 16, no. 4 (2021): e0247743. http://dx.doi.org/10.1371/journal.pone.0247743.

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A large number of GPCRs are potentially valuable drug targets but remain understudied. Many of these lack well-validated activating ligands and are considered “orphan” receptors, and G protein coupling profiles have not been defined for many orphan GPCRs. Here we asked if constitutive receptor activity can be used to determine G protein coupling profiles of orphan GPCRs. We monitored nucleotide-sensitive interactions between 48 understudied orphan GPCRs and five G proteins (240 combinations) using bioluminescence resonance energy transfer (BRET). No receptor ligands were used, but GDP was used

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Rodríguez Sarmiento, Deisy Yurley. "Beyond reproduction: Exploring the Non-Canonical roles of the Kisspeptin System in Diverse Biological Systems." Bionatura 8, no. 3 (2023): 1–6. http://dx.doi.org/10.21931/rb/2023.08.03.13.

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G protein-coupled receptors are integral membrane proteins in cell signaling processes. Activation of G protein-coupled receptors by specific agonists promotes the activation of different G-proteins, activating different intracellular signaling pathways, including adenylate cyclase activation and intracellular calcium release. One of the G protein-coupled receptors studied is the kisspeptin receptor, which regulates reproduction and gonadotropin secretion. However, recent studies have shown that kisspeptin and its receptor have non-canonical roles in cell signaling and several biological syste

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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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18

Morfis, Maria, Nanda Tilakaratne, Sebastian G. B. Furness, et al. "Receptor Activity-Modifying Proteins Differentially Modulate the G Protein-Coupling Efficiency of Amylin Receptors." Endocrinology 149, no. 11 (2008): 5423–31. http://dx.doi.org/10.1210/en.2007-1735.

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Receptor activity-modifying proteins (RAMPs) 1, 2, and 3 are prototypic G protein-coupled receptor accessory proteins that can alter not only receptor trafficking but also receptor phenotype. Specific RAMP interaction with the calcitonin receptor (CTR) generates novel and distinct receptors for the peptide amylin; however, the role of RAMPs in receptor signaling is not understood. The current study demonstrates that RAMP interaction with the CTRa in COS-7 or HEK-293 cells leads to selective modulation of signaling pathways activated by the receptor complex. There was a 20- to 30-fold induction

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Claing, Audrey. "Regulation of G protein-coupled receptor endocytosis by ARF6 GTP-binding proteins." Biochemistry and Cell Biology 82, no. 6 (2004): 610–17. http://dx.doi.org/10.1139/o04-113.

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The function of G protein-coupled receptors is regulated by a broad variety of membrane-bound and intracellular proteins. These act in concert to activate signaling pathways that will lead to the desensitization of activated receptors and, for most receptor types, their trafficking to intracellular compartments. This review focuses mainly on the endocytic pathways used by a G protein-coupled receptor and on the proteins that play an essential role in the regulation of the internalization process, most specifically the ADP-ribosylation factors. This family of proteins has been shown to be impor

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Mika, Kaan, Steeve Cruchet, Phing Chian Chai, et al. "Olfactory receptor–dependent receptor repression in Drosophila." Science Advances 7, no. 32 (2021): eabe3745. http://dx.doi.org/10.1126/sciadv.abe3745.

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In olfactory systems across phyla, most sensory neurons express a single olfactory receptor gene selected from a large genomic repertoire. We describe previously unknown receptor gene–dependent mechanisms that ensure singular expression of receptors encoded by a tandem gene array [Ionotropic receptor 75c (Ir75c), Ir75b, and Ir75a, organized 5′ to 3′] in Drosophila melanogaster. Transcription from upstream genes in the cluster runs through the coding region of downstream loci and inhibits their expression in cis, most likely via transcriptional interference. Moreover, Ir75c blocks accumulation

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LEUTHÄUSER, Kerstin, Remo GUJER, Amaya ALDECOA, et al. "Receptor-activity-modifying protein 1 forms heterodimers with two G-protein-coupled receptors to define ligand recognition." Biochemical Journal 351, no. 2 (2000): 347–51. http://dx.doi.org/10.1042/bj3510347.

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Receptor-activity-modifying proteins (RAMPs) with single transmembrane domains define the function of two G-protein-coupled receptors of the B family. Cell-surface complexes of human RAMP1 (hRAMP1) and human calcitonin (CT) receptor isotype 2 (hCTR2) or rat CT-receptor-like receptor (rCRLR) have now been identified through protein cross-linking, co-immunoprecipitation and confocal microscopy. They are two distinct CT-gene-related peptide (CGRP) receptors coupled to cAMP production and pharmacologically distinguished by the CT and CGRP antagonists salmon CT(8-32) and human or rat CGRP(8-37). Th

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Levin, E. R. "Natriuretic peptide C-receptor: more than a clearance receptor." American Journal of Physiology-Endocrinology and Metabolism 264, no. 4 (1993): E483—E489. http://dx.doi.org/10.1152/ajpendo.1993.264.4.e483.

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The natriuretic peptide family of proteins acts through two distinct classes of receptors that signal through entirely different mechanisms. The elucidation of the structure of the guanylate cyclase-containing receptor proteins has provided a better understanding of the mechanisms by which the natriuretic peptides regulate diverse functions of salt and water balance, in conjunction with other vasoactive peptides. A second receptor class was named for the originally described function of this protein to clear the natriuretic peptides from plasma. The mechanism of signaling for the natriuretic p

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BÖHM, Stephan K., Eileen F. GRADY, and Nigel W. BUNNETT. "Regulatory mechanisms that modulate signalling by G-protein-coupled receptors." Biochemical Journal 322, no. 1 (1997): 1–18. http://dx.doi.org/10.1042/bj3220001.

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The large and functionally diverse group of G-protein-coupled receptors includes receptors for many different signalling molecules, including peptide and non-peptide hormones and neurotransmitters, chemokines, prostanoids and proteinases. Their principal function is to transmit information about the extracellular environment to the interior of the cell by interacting with the heterotrimeric G-proteins, and they thereby participate in many aspects of regulation. Cellular responses to agonists of these receptors are usually rapidly attenuated. Mechanisms of signal attenuation include removal of

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Moores, Sheri L., Laura M. Selfors, Jessica Fredericks, et al. "Vav Family Proteins Couple to Diverse Cell Surface Receptors." Molecular and Cellular Biology 20, no. 17 (2000): 6364–73. http://dx.doi.org/10.1128/mcb.20.17.6364-6373.2000.

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ABSTRACT Vav proteins are guanine nucleotide exchange factors for Rho family GTPases which activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. Vav proteins contain several protein binding domains which can link cell surface receptors to downstream signaling proteins. Vav1 is expressed exclusively in hematopoietic cells and tyrosine phosphorylated in response to activation of multiple cell surface receptors. However, it is not known whether the recently identified isoforms Vav2 and Vav3, which are broadly expressed, can couple with similar classes of

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Valentine, Cathleen D., та Peter M. Haggie. "Confinement of β1- and β2-adrenergic receptors in the plasma membrane of cardiomyocyte-like H9c2 cells is mediated by selective interactions with PDZ domain and A-kinase anchoring proteins but not caveolae". Molecular Biology of the Cell 22, № 16 (2011): 2970–82. http://dx.doi.org/10.1091/mbc.e11-01-0034.

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The sympathetic nervous system regulates cardiac output by activating adrenergic receptors (ARs) in cardiac myocytes. The predominant cardiac ARs, β1- and β2AR, are structurally similar but mediate distinct signaling responses. Scaffold protein–mediated compartmentalization of ARs into discrete, multiprotein complexes has been proposed to dictate differential signaling responses. To test the hypothesis that βARs integrate into complexes in live cells, we measured receptor diffusion and interactions by single-particle tracking. Unstimulated β1- and β2AR were highly confined in the membrane of H

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GAO, Zhenhai, Anna S. ROBEVA, and Joel LINDEN. "Purification of A1 adenosine receptor–G-protein complexes: effects of receptor down-regulation and phosphorylation on coupling." Biochemical Journal 338, no. 3 (1999): 729–36. http://dx.doi.org/10.1042/bj3380729.

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We examined the effects of exposing A1 adenosine receptors (A1ARs) to an agonist on the stability and phosphorylation state of receptor–guanine nucleotide-binding regulatory protein (R–G-protein) complexes. Non-denatured recombinant human A1ARs extended on the N-terminus with hexahistidine (His6) and the FLAG (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys) epitope (H/F) were purified to near homogeneity from stably transfected Chinese-hamster ovary (CHO)-K1 cells. Purified receptors have pharmacological properties similar to receptors in membranes. G-proteins were co-purified with 15±2% of H/F-A1AR unless r

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Raymond, J. R. "Multiple mechanisms of receptor-G protein signaling specificity." American Journal of Physiology-Renal Physiology 269, no. 2 (1995): F141—F158. http://dx.doi.org/10.1152/ajprenal.1995.269.2.f141.

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The hormone-receptor-G protein complex transduces extracellular information into intracellular signals that ultimately regulate cellular functions in a highly specific manner. There are hundreds of receptor types that transduce signals through a relatively limited repertoire of heterotrimeric G proteins. Linear models of signaling specificity that require specific and highly selective coupling of hormone to receptor to G protein have proven inadequate to explain how highly particular signals are funneled through the G protein "bottleneck." Recent studies have uncovered a plethora of mechanisms

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Snitkovsky, Sophie, Thomas M. J. Niederman, Richard C. Mulligan, and John A. T. Young. "Targeting Avian Leukosis Virus Subgroup A Vectors by Using a TVA-VEGF Bridge Protein." Journal of Virology 75, no. 3 (2001): 1571–75. http://dx.doi.org/10.1128/jvi.75.3.1571-1575.2001.

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ABSTRACT Previously, we have demonstrated that bridge proteins comprised of avian leukosis virus (ALV) receptors fused to epidermal growth factor (EGF) can be used to selectively target retroviral vectors with ALV envelope proteins to cells expressing EGF receptors. To determine whether another type of ligand incorporated into an ALV receptor-containing bridge protein can also function to target retroviral infection, the TVA-VEGF110 bridge protein was generated. TVA-VEGF110 consists of the extracellular domain of the TVA receptor for ALV subgroup A (ALV-A), fused via a proline-rich linker pept

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Vlassara, H., M. Brownlee, and A. Cerami. "Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors." Journal of Experimental Medicine 164, no. 4 (1986): 1301–9. http://dx.doi.org/10.1084/jem.164.4.1301.

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A high-affinity macrophage receptor has been identified that recognizes proteins modified by a common in vivo process, long-term nonenzymatic reaction of glucose with proteins (AGE proteins). This receptor for glucose-modified proteins is now shown to be distinct from previously described scavenger receptors, using competition and crosscompetition experiments between AGE-modified protein and a variety of in vitro-modified scavenger receptor ligands, including unmodified BSA, unmodified low-density lipoproteins (LDL), acetyl-LDL, maleyl-BSA, and formaldehyde-treated BSA. Furthermore, the specif

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Eishingdrelo, Haifeng, Wei Sun, Hua Li та ін. "ERK and β-Arrestin Interaction". Journal of Biomolecular Screening 20, № 3 (2014): 341–49. http://dx.doi.org/10.1177/1087057114557233.

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β-Arrestin, a signal adaptor protein, mediates intracellular signal transductions through protein-protein interactions by bringing two or more proteins in proximity. Extracellular signal-regulated kinase (ERK), a protein kinase in the family of mitogen-activated protein kinases (MAPKs), is involved in various receptor signal pathways. Interaction of ERK with β-arrestin or formation of ERK/β-arrestin signal complex occurs in response to activation of a variety of cell surface receptors. The ERK/β-arrestin signal complex may be a common transducer to converge a variety of extracellular stimuli t

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Barnathan, ES, A. Kuo, K. Kariko, et al. "Characterization of human endothelial cell urokinase-type plasminogen activator receptor protein and messenger RNA." Blood 76, no. 9 (1990): 1795–806. http://dx.doi.org/10.1182/blood.v76.9.1795.bloodjournal7691795.

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Human umbilical vein endothelial cells in culture (HUVEC) express receptors for urokinase-type plasminogen activators (u-PA). The immunochemical nature of this receptor and its relationship to u-PA receptors expressed by other cell types is unknown. Cross-linking active site-blocked u-PA to HUVEC lead to an increase in its apparent molecular mass by approximately 40 Kd. The predominant u-PA binding protein isolated from whole cell detergent extracts migrated with a molecular mass of approximately 36 Kd using affinity chromatography. In contrast, when only cell surface proteins were radiolabele

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Lustofin, Sylwia, Alicja Kamińska, Małgorzata Brzoskwinia, et al. "Nuclear and Membrane Receptors for Sex Steroids Are Involved in the Regulation of Delta/Serrate/LAG-2 Proteins in Rodent Sertoli Cells." International Journal of Molecular Sciences 23, no. 4 (2022): 2284. http://dx.doi.org/10.3390/ijms23042284.

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Delta/Serrate/LAG-2 (DSL) proteins, which serve as ligands for Notch receptors, mediate direct cell–cell interactions involved in the determination of cell fate and functioning. The present study aimed to explore the role of androgens and estrogens, and their receptors in the regulation of DSL proteins in Sertoli cells. To this end, primary rat Sertoli cells and TM4 Sertoli cell line were treated with either testosterone or 17β-estradiol and antagonists of their receptors. To confirm the role of particular receptors, knockdown experiments were performed. mRNA and protein expressions of Jagged1

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Wicher, Dieter, and Fabio Miazzi. "Functional properties of insect olfactory receptors: ionotropic receptors and odorant receptors." Cell and Tissue Research 383, no. 1 (2021): 7–19. http://dx.doi.org/10.1007/s00441-020-03363-x.

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AbstractThe majority of insect olfactory receptors belong to two distinct protein families, the ionotropic receptors (IRs), which are related to the ionotropic glutamate receptor family, and the odorant receptors (ORs), which evolved from the gustatory receptor family. Both receptor types assemble to heteromeric ligand-gated cation channels composed of odor-specific receptor proteins and co-receptor proteins. We here present in short the current view on evolution, function, and regulation of IRs and ORs. Special attention is given on how their functional properties can meet the environmental a

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Chatterjee, Tapan K., and Rory A. Fisher. "Multiple affinity and guanine nucleotide sensitive forms of the calcitonin gene related peptide (CGRP) receptor." Canadian Journal of Physiology and Pharmacology 73, no. 7 (1995): 968–73. http://dx.doi.org/10.1139/y95-134.

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Calcitonin gene related peptide (CGRP) is a novel neuropeptide with an impressive array of biological actions consistent with its diverse tissue distribution and suggested role as neurotransmitter or neuromodulator. Binding sites for CGRP with properties consistent with those of receptors are present in both central and peripheral tissues. Radioligand binding studies were performed to investigate the fundamental processes underlying CGRP receptor activation and signaling following agonist occupancy of the receptor. These studies documented the existence of a selective, high affinity, and homog

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Shi, Xuan-Zheng, and Sushil K. Sarna. "G protein-mediated dysfunction of excitation-contraction coupling in ileal inflammation." American Journal of Physiology-Gastrointestinal and Liver Physiology 286, no. 6 (2004): G899—G905. http://dx.doi.org/10.1152/ajpgi.00408.2003.

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Inflammation impairs the circular muscle contractile response to muscarinic (M) receptor activation. The aim of this study was to investigate whether the expression of muscarinic receptors, their binding affinity, and the expression and activation of receptor-coupled G proteins contribute to the suppression of contractility in inflammation. The studies were performed on freshly dissociated single smooth muscle cells from normal and inflamed canine ileum. Northern blotting indicated the presence of only M2 and M3 receptors on canine ileal circular muscle cells. Inflammation did not alter the mR

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Udawela, Madhara, Debbie L. Hay, and Patrick M. Sexton. "The receptor activity modifying protein family of G protein coupled receptor accessory proteins." Seminars in Cell & Developmental Biology 15, no. 3 (2004): 299–308. http://dx.doi.org/10.1016/j.semcdb.2003.12.019.

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Johnstone, Elizabeth K. M., and Kevin D. G. Pfleger. "Profiling novel pharmacology of receptor complexes using Receptor-HIT." Biochemical Society Transactions 49, no. 4 (2021): 1555–65. http://dx.doi.org/10.1042/bst20201110.

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Many receptors are able to undergo heteromerisation, leading to the formation of receptor complexes that may have pharmacological profiles distinct from those of the individual receptors. As a consequence of this, receptor heteromers can be classed as new drug targets, with the potential for achieving greater specificity and selectivity over targeting their constituent receptors. We have developed the Receptor-Heteromer Investigation Technology (Receptor-HIT), which enables the detection of receptor heteromers using a proximity-based reporter system such as bioluminescence resonance energy tra

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Michinaga, Shotaro, Ayaka Nagata, Ryosuke Ogami, Yasuhiro Ogawa, and Shigeru Hishinuma. "Histamine H1 Receptor-Mediated JNK Phosphorylation Is Regulated by Gq Protein-Dependent but Arrestin-Independent Pathways." International Journal of Molecular Sciences 25, no. 6 (2024): 3395. http://dx.doi.org/10.3390/ijms25063395.

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Arrestins are known to be involved not only in the desensitization and internalization of G protein-coupled receptors but also in the G protein-independent activation of mitogen-activated protein (MAP) kinases, such as extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK), to regulate cell proliferation and inflammation. Our previous study revealed that the histamine H1 receptor-mediated activation of ERK is dually regulated by Gq proteins and arrestins. In this study, we investigated the roles of Gq proteins and arrestins in the H1 receptor-mediated activation of JNK i

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Żuk, Justyna, Damian Bartuzi, Przemysław Miszta, and Agnieszka A. Kaczor. "The Role of Lipids in Allosteric Modulation of Dopamine D2 Receptor—In Silico Study." Molecules 27, no. 4 (2022): 1335. http://dx.doi.org/10.3390/molecules27041335.

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The dopamine D2 receptor, belonging to the class A G protein-coupled receptors (GPCRs), is an important drug target for several diseases, including schizophrenia and Parkinson’s disease. The D2 receptor can be activated by the natural neurotransmitter dopamine or by synthetic ligands, which in both cases leads to the receptor coupling with a G protein. In addition to receptor modulation by orthosteric or allosteric ligands, it has been shown that lipids may affect the behaviour of membrane proteins. We constructed a model of a D2 receptor with a long intracellular loop (ICL3) coupled with Giα1

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Smith, D. M., H. A. Coppock, D. J. Withers, et al. "Adrenomedullin: receptor and signal transduction." Biochemical Society Transactions 30, no. 4 (2002): 432–37. http://dx.doi.org/10.1042/bst0300432.

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Adrenomedullin is a vascular tissue peptide and a member of the calcitonin family of peptides, which includes calcitonin, calcitonin-gene-related peptide (CGRP) and amylin. Its many biological actions are mediated via CGRP type 1 (CGRP1) receptors and by specific adrenomedullin receptors. Although the pharmacology of these receptors is distinct, they are both represented in molecular terms by the type II family G-protein-coupled receptor, calcitonin-receptor-like receptor (CRLR). The specificity here is defined by co-expression of receptor-activity-modifying proteins (RAMPs). CGRP1 receptors a

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King, M. J., and G. J. Sale. "Insulin-receptor phosphotyrosyl-protein phosphatases." Biochemical Journal 256, no. 3 (1988): 893–902. http://dx.doi.org/10.1042/bj2560893.

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Calmodulin-dependent protein phosphatase has been proposed to be an important phosphotyrosyl-protein phosphatase. The ability of the enzyme to attack autophosphorylated insulin receptor was examined and compared with the known ability of the enzyme to act on autophosphorylated epidermal-growth-factor (EGF) receptor. Purified calmodulin-dependent protein phosphatase was shown to catalyse the complete dephosphorylation of phosphotyrosyl-(insulin receptor). When compared at similar concentrations, 32P-labelled EGF receptor was dephosphorylated at greater than 3 times the rate of 32P-labelled insu

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Morello, Jean-Pierre, and Michel Bouvier. "Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors." Biochemistry and Cell Biology 74, no. 4 (1996): 449–57. http://dx.doi.org/10.1139/o96-049.

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Protein acylation is a post-translational modification that has seized much attention in the last few years. Depending on the nature of the fatty acid added, protein acylation can take the form of palmitoylation, myristoylation, or prenylation. Palmitoylation has been implicated in the modification of several different proteins and is particularly prevalent in G-protein coupled receptors and their cognate G-proteins, where it is thought to have an important regulatory function. Given that palmitoylation of these proteins is a dynamic phenomenon in which turnover rate is modulated by agonist ac

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Staus, Dean P., Laura M. Wingler, Minjung Choi та ін. "Sortase ligation enables homogeneous GPCR phosphorylation to reveal diversity in β-arrestin coupling". Proceedings of the National Academy of Sciences 115, № 15 (2018): 3834–39. http://dx.doi.org/10.1073/pnas.1722336115.

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The ability of G protein-coupled receptors (GPCRs) to initiate complex cascades of cellular signaling is governed by the sequential coupling of three main transducer proteins, G protein, GPCR kinase (GRK), and β-arrestin. Mounting evidence indicates these transducers all have distinct conformational preferences and binding modes. However, interrogating each transducer’s mechanism of interaction with GPCRs has been complicated by the interplay of transducer-mediated signaling events. For example, GRK-mediated receptor phosphorylation recruits and induces conformational changes in β-arrestin, wh

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Horiuchi, Masatsugu, Jun Iwanami, and Masaki Mogi. "Regulation of angiotensin II receptors beyond the classical pathway." Clinical Science 123, no. 4 (2012): 193–203. http://dx.doi.org/10.1042/cs20110677.

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The RAS (renin–angiotensin system) plays a role not only in the cardiovascular system, including blood pressure regulation, but also in the central nervous system. AngII (angiotensin II) binds two major receptors: the AT1 receptor (AngII type 1 receptor) and AT2 receptor (AngII type 2 receptor). It has been recognized that AT2 receptor activation not only opposes AT1 receptor actions, but also has unique effects beyond inhibitory cross-talk with AT1 receptor signalling. Novel pathways beyond the classical actions of RAS, the ACE (angiotensin-converting enzyme)/AngII/AT1 receptor axis, have bee

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Fardoun, Riham Zein, Mohammad Asghar, and Mustafa Lokhandwala. "Role of oxidative stress in defective renal dopamine D1 receptor-G protein coupling and function in old Fischer 344 rats." American Journal of Physiology-Renal Physiology 291, no. 5 (2006): F945—F951. http://dx.doi.org/10.1152/ajprenal.00111.2006.

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Aging is associated with an increase in oxidative stress. Previously, we have reported that dopamine failed to inhibit proximal tubular Na-K-ATPase and to promote sodium excretion in old rats (Beheray S, Kansra V, Hussain T, and Lokhandwala MF. Kidney Int 58: 712–720, 2000). This was due to uncoupling of dopamine D1 receptors from G proteins resulting from hyperphosphorylation of D1 receptors. The present study was designed to test the role of oxidative stress in the age-related decline in renal dopamine D1 receptor function. We observed that old animals had increased malondialdehyde (MDA) lev

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Escobedo, J. A., D. R. Kaplan, W. M. Kavanaugh, C. W. Turck, and L. T. Williams. "A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine." Molecular and Cellular Biology 11, no. 2 (1991): 1125–32. http://dx.doi.org/10.1128/mcb.11.2.1125-1132.1991.

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Platelet-derived growth factor (PDGF) stimulates autophosphorylation of the PDGF receptor and association of the receptor with several cytoplasmic molecules, including phosphatidylinositol-3 kinase (PI3 kinase). In this study we examined the association of PI3 kinase with immunoprecipitated autophosphorylated PDGF receptor in vitro. The PI3 kinase from cell lysates bound to the wild-type receptor but not to a mutant receptor that had a deletion of the kinase insert region. A protein of an apparent size of 85 kDa bound to the receptor, consistent with previous observations that a protein of thi

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Escobedo, J. A., D. R. Kaplan, W. M. Kavanaugh, C. W. Turck, and L. T. Williams. "A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine." Molecular and Cellular Biology 11, no. 2 (1991): 1125–32. http://dx.doi.org/10.1128/mcb.11.2.1125.

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Platelet-derived growth factor (PDGF) stimulates autophosphorylation of the PDGF receptor and association of the receptor with several cytoplasmic molecules, including phosphatidylinositol-3 kinase (PI3 kinase). In this study we examined the association of PI3 kinase with immunoprecipitated autophosphorylated PDGF receptor in vitro. The PI3 kinase from cell lysates bound to the wild-type receptor but not to a mutant receptor that had a deletion of the kinase insert region. A protein of an apparent size of 85 kDa bound to the receptor, consistent with previous observations that a protein of thi

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Matthews, Sharon A., Enrique Rozengurt, and Doreen Cantrell. "Protein Kinase D." Journal of Experimental Medicine 191, no. 12 (2000): 2075–82. http://dx.doi.org/10.1084/jem.191.12.2075.

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Protein kinase Cs (PKCs) are activated by antigen receptors in lymphocytes, but little is known about proximal targets for PKCs in antigen receptor–mediated responses. In this report, we define a role for diacylglycerol-regulated PKC isoforms in controlling the activity of the serine/threonine kinase protein kinase D (PKD; also known as PKCμ) in T cells, B cells, and mast cells. Antigen receptor activation of PKD is a rapid and sustained response that can be seen in T cells activated via the T cell antigen receptor, B cells activated via the B cell antigen receptor, and in mast cells triggered

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Levin, Ellis R. "Bidirectional Signaling between the Estrogen Receptor and the Epidermal Growth Factor Receptor." Molecular Endocrinology 17, no. 3 (2003): 309–17. http://dx.doi.org/10.1210/me.2002-0368.

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Abstract Interactions between the estrogen receptor (ER) and the epidermal growth factor receptor (EGFR) contribute to the biological effects of these binding protein families. EGFR stimulates DNA synthesis and gene transcription in the uterus, related in part to estrogen-independent activation of the nuclear ER. This results from signal transduction enacted by the plasma membrane tyrosine kinase growth factor receptor, leading to 1) phosphorylation and activation of the nuclear ER, and 2) phosphorylation of coregulator proteins. More recently, it has been shown that a pool of ERα resides in o

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Zhang, Zheng, Fen Yu, Yuanqiang Zou, et al. "Phage protein receptors have multiple interaction partners and high expressions." Bioinformatics 36, no. 10 (2020): 2975–79. http://dx.doi.org/10.1093/bioinformatics/btaa123.

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Abstract Motivation Receptors on host cells play a critical role in viral infection. How phages select receptors is still unknown. Results Here, we manually curated a high-quality database named phageReceptor, including 427 pairs of phage–host receptor interactions, 341 unique viral species or sub-species and 69 bacterial species. Sugars and proteins were most widely used by phages as receptors. The receptor usage of phages in Gram-positive bacteria was different from that in Gram-negative bacteria. Most protein receptors were located on the outer membrane. The phage protein receptors (PPRs) w

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