Cited by 456Receptor Mechanisms and SignalingCellular transport and secretionNeuropeptides and Animal Physiology

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Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-β-arrestin complexes after receptor endocytosis

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Oakley, Robert H., Laporte, Stéphane A., Holt, Jason A., Barak, Larry S., Caron, Marc G.·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m101450200

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Abstract

beta-Arrestins bind agonist-activated G protein-coupled receptors (GPCRs) and mediate their desensitization and internalization. Although beta-arrestins dissociate from some receptors at the plasma membrane, such as the beta2 adrenergic receptor, they remain associated with other GPCRs and internalize with them into endocytic vesicles. Formation of stable receptor-beta-arrestin complexes that persist inside the cell impedes receptor resensitization, and the aberrant formation of these complexes may play a role in GPCR-based diseases (Barak, L. S., Oakley, R. H., Laporte, S. A., and Caron, M. G. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 93-98). Here, we investigate the molecular determinants responsible for sustained receptor/beta-arrestin interactions. We show in real time and in live human embryonic kidney (HEK-293) cells that a beta-arrestin-2-green fluorescent protein conjugate internalizes into endocytic vesicles with agonist-activated neurotensin-1 receptor, oxytocin receptor, angiotensin II type 1A receptor, and substance P receptor. Using receptor mutagenesis, we demonstrate that the ability of beta-arrestin to remain associated with these receptors is mediated by specific clusters of serine and threonine residues located in the receptor carboxyl-terminal tail. These clusters are remarkably conserved in their position within the carboxyl-terminal domain and serve as primary sites of agonist-dependent receptor phosphorylation. In addition, we identify a beta-arrestin mutant with enhanced affinity for the agonist-activated beta2-adrenergic receptor that traffics into endocytic vesicles with receptors that lack serine/threonine clusters and normally dissociate from wild-type beta-arrestin at the plasma membrane. By identifying receptor and beta-arrestin residues critical for the formation of stable receptor-beta-arrestin complexes, these studies provide novel targets for regulating GPCR responsiveness and treating diseases resulting from abnormal GPCR/beta-arrestin interactions.

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Background
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BackgroundInfluential
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Background
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Background
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“OTRs have previously been shown to congregate with β-arrestin following activation into defined punctuated regions of the plasma membrane, which suggest that they are targeted into clathrin-coated pits for internalization.(31,50) OTRs are also highly expressed in the cholesterol-rich, caveolin-containing membrane doma…”
Background
Inhibition of Chemoattractant N‐Formyl Peptide Receptor Trafficking by Active Arrestins
Key, T. A., Vines, C. M., Wagener, B. M., Gurevich, V. V., Sklar, L. A., & Prossnitz, E. R. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.00248.x · Cited by 24
“High agonist affinity complexes of arrestin-2–3A with phosphorylated forms of the FPR Arrestin-2 contains a series of consecutive amino acids in the carboxy-terminus with bulky, hydrophobic side chains (Ile386 Val387 Phe388).”
Background
Arrestin Variants Display Differential Binding Characteristics for the Phosphorylated N-Formyl Peptide Receptor Carboxyl Terminus
Potter, R. M., Key, T. A., Gurevich, V. V., Sklar, L. A., & Prossnitz, E. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111086200 · Cited by 24
Mdm2-mediated ubiquitination of PKCβII in the nucleus mediates clathrin-mediated endocytic activity
Min, X., Zhang, X., Sun, N., Acharya, S., & Kim, K. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113675 · Cited by 23
3.1 Molecular Pharmacology of the Dopamine Receptors
Rankin, M. L., Hazelwood, L. A., Free, R. B., Namkung, Y., Rex, E., Roof, R. A., & Sibley, D. R. (2009) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780195373035.003.0006 · Cited by 25
Synthesis, characterization and in vitro cytotoxicity studies of a macromolecular conjugate of paclitaxel bearing oxytocin as targeting moiety
Cavallaro, G., Maniscalco, L., Campisi, M., Schillaci, D., & Giammona, G. (2006) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2006.10.013 · Cited by 23
Receptor tyrosine kinase and G‐protein coupled receptor signaling and sorting within endosomes
Grimes, M. L., & Miettinen, H. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01603.x · Cited by 23
“…studies with V2R, AT1aR, neurotensin-1 receptor (NTR-1) and oxytocin receptor (OTR) indicate that the affinity of barr to these receptors is regulated by the cytoplasmic tail sequences, specifically within clusters of serine and threonine residues (SS, STS, SSS, SSXS) (Oakley et al. 2001).”
Background
A Split Luciferase Complementation Assay for the Quantification of β-Arrestin2 Recruitment to Dopamine D2-Like Receptors
Forster, L., Grätz, L., Mönnich, D., Bernhardt, G., & Pockes, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176103 · Cited by 22
Trans-Golgi Network (TGN) as a Regulatory Node for β1-Adrenergic Receptor (β1AR) Down-modulation and Recycling
Cheng, S., & Filardo, E. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323782 · Cited by 22
Analysis of temporal patterns of GPCR–β-arrestin interactions using split luciferase-fragment complementation
Hattori, M., Tanaka, M., Takakura, H., Aoki, K., Miura, K., Anzai, T., & Ozawa, T. (2012) · Molecular BioSystems · doi:10.1039/c2mb25443c · Cited by 22
Angiotensin II receptors and peritoneal dialysis-induced peritoneal fibrosis
Morinelli, T. A., Luttrell, L. M., Strungs, E. G., & Ullian, M. E. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.04.016 · Cited by 22
“Not surprisingly then, GPCRs are the single most common target of drugs in clinical use (3).”
BackgroundInfluential
Regulation of Membrane Cholecystokinin-2 Receptor by Agonists Enables Classification of Partial Agonists as Biased Agonists
Magnan, R., Masri, B., Escrieut, C., Foucaud, M., Cordelier, P., & Fourmy, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.196048 · Cited by 22
Role of Rhodopsin and Arrestin Phosphorylation in Retinal Degeneration of Drosophila
Kristaponyte, I., Hong, Y., Lu, H., & Shieh, B. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0565-12.2012 · Cited by 22
Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonist-induced beta-arrestin1 recruitment but differs from the apparent principal phosphorylation site
Neuschäfer‐Rube, F., Hermosilla, R., REHWALD, M., Rönnstrand, L., Schülein, R., Wernstedt, C., & Püschel, G. P. (2004) · Biochemical Journal · doi:10.1042/bj20031820 · Cited by 22
Functional consequences of spatial, temporal and ligand bias of G protein-coupled receptors
Tóth, A. D., Turu, G., & Hunyady, L. (2024) · Nature Reviews Nephrology · doi:10.1038/s41581-024-00869-3 · Cited by 22
“The strength of the interaction between receptors and β-arrestins is mainly determined by the abundance of phosphorylated serine/ threonine-rich motifs in the C terminus or ICL3 region of the GPCR 46,47 .”
Discrete GPCR-triggered endocytic modes enable β-arrestins to flexibly regulate cell signaling
Barsi‐Rhyne, B., Manglik, A., & von Zastrow, M. (2022) · eLife · doi:10.7554/elife.81563 · Cited by 23
Molecular determinants of orexin receptor‐arrestin‐ubiquitin complex formation
Jaeger, W. C., Seeber, R. M., Eidne, K. A., & Pfleger, K. D. G. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12481 · Cited by 21
“Residues indicated in bold are in the serine/threonine (S/T) clusters that were assessed as putative GRK phosphorylation sites (Oakley et al., 2001).”
BackgroundInfluential
Cell-type-specific pathways of neurotensin endocytosis
Savdie, C., Ferguson, S. S. G., Vincent, J., Beaudet, A., & Stroh, T. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-0102-3 · Cited by 25
“Accordingly, like other non-recycling receptors, NTS1 is internalized together with β–arrestin following stimulation with neurotensin (Zhang et al. 1999; Oakley et al. 2000, 2001).”
BackgroundInfluential
Depletion of β‐arrestin2 in hepatic stellate cells reduces cell proliferation via ERK pathway
Sun, W., Song, Y., Hu, S., Wang, Q., Wu, H., Chen, J., & Wei, W. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24458 · Cited by 21
“Arrestins are known to promote receptor desensitization and internalization by interacting with the phosphorylated form of GPCRs, thereby preventing their coupling with G protein [Oakley et al., 2001; Liggett, 2011].”
Background
The Ligand‐Independent Translocation Assay: An Enabling Technology for Screening Orphan G Protein‐Coupled Receptors by Arrestin Recruitment
Oakley, R. H., Hudson, C. C., Sjaastad, M. D., & Loomis, C. R. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)14004-5 · Cited by 21
Involvement of a cytoplasmic-tail serine cluster in urotensin II receptor internalization
Proulx, C. D., Simaan, M., Escher, E., Laporte, S. A., Guillemette, G., & Leduc, R. (2004) · Biochemical Journal · doi:10.1042/bj20040807 · Cited by 21
Different conformational dynamics of various active states of β-arrestin1 analyzed by hydrogen/deuterium exchange mass spectrometry
Kim, D. K., Yun, Y., Kim, H. R., Seo, M., & Chung, K. Y. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.04.006 · Cited by 20
Role of PTH1R internalization in osteoblasts and bone mass using a phosphorylation-deficient knock-in mouse model
Datta, N. S., Samra, T. A., Mahalingam, C. D., Datta, T., & Abou‐Samra, A. (2010) · Journal of Endocrinology · doi:10.1677/joe-10-0227 · Cited by 20
“…C-terminal serine and threonine residues of agonist-stimulated GPCRs and binding of the members of the b-arrestins (Pitcher et al. 1998, Oakley et al. 2001). b-Arrestin 1 and 2 knockout mice and transgenic mice with targeted overexpression of a peptide inhibitor of GRK2 have been used…”
Different Mechanisms Regulate Lysophosphatidic Acid (LPA)-dependent Versus Phorbol Ester-dependent Internalization of the LPA1 Receptor
Urs, N. M., Kowalczyk, A. P., & Radhakrishna, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m710003200 · Cited by 20
Synthesis andin vitrocharacterization of oxytocin receptor targeted PEGylated immunoliposomes for drug delivery to the uterus
Hua, S. (2018) · Journal of Liposome Research · doi:10.1080/08982104.2018.1556293 · Cited by 19
Neurons expressing serotonin-1B receptor in the basolateral nuclear group of the amygdala in normally behaving and aggressive dogs
Jacobs, C., Broeck, W. V. D., & Simoens, P. (2007) · Brain Research · doi:10.1016/j.brainres.2006.11.096 · Cited by 19
Migration mediated by the oxysterol receptor GPR183 depends on arrestin coupling but not receptor internalization
Kjær, V. M. S., Daugvilaite, V., Stępniewski, T. M., Madsen, C. M., Jørgensen, A. S., Bhuskute, K. R., Inoue, A., Ulven, T., Benned‐Jensen, T., Hjorth, S. A., et al. (2023) · Science Signaling · doi:10.1126/scisignal.abl4283 · Cited by 18
Agonist-induced changes in RalA activities allows the prediction of the endocytosis of G protein-coupled receptors
Zheng, M., Zhang, X., Guo, S., Zhang, X., Min, C., Cheon, S. H., Oak, M., Kim, Y. R., & Kim, K. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.10.007 · Cited by 18
Desensitization of human CRF2(a) receptor signaling governed by agonist potency and βarrestin2 recruitment
Hauger, R. L., Olivares-Reyes, J. A., Braun, S. L., Hernández-Aranda, J., Hudson, C. C., Gutknecht, E., Dautzenberg, F. M., & Oakley, R. H. (2013) · Regulatory Peptides · doi:10.1016/j.regpep.2013.06.009 · Cited by 18
“dishes (MatTek, Ashland, MA) and cultured overnight using a previously published protocol [15,24].”
The association of single-nucleotide polymorphisms in the oxytocin receptor and G protein–coupled receptor kinase 6 (GRK6) genes with oxytocin dosing requirements and labor outcomes
Grotegut, C. A., Ngan, E., Garrett, M. E., Miranda, M. L., Ashley‐Koch, A. E., & Swamy, G. K. (2017) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2017.05.023 · Cited by 18
“SEPTEMBER 2017 Ameri kinase 6 (GRK6), a member of the G proteinecoupled receptor kinase (GRK) family, allowing for the recruitment of barrestin, which leads to receptor internalization and desensitization.(9-12) As an entire class, GPCRs are prone to GRKmediated, b-arrestin-dependent desensitization.”
Background
G Protein-Coupled Receptor Desensitization as a Measure of Signaling: Modeling of Arrestin Recruitment to Activated CCK-B Receptors
Barak, L. S., Oakley, R. H., & Shetzline, M. A. (2003) · Assay and Drug Development Technologies · doi:10.1089/154065803322163722 · Cited by 18
“29 To determine if the kinetics of arrestin dissociation from the CCK-B receptor was similarly rapid, arrestin-GFP dissociation from gastrin-activated CCK-B receptors was measured after treatment with L-365,260 (Fig.”
β-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface
Strous, G. J., & Schantl, J. (2001) · Science s STKE · doi:10.1126/stke.2001.110.pe41 · Cited by 18
“shortly after endocytosis (27), allowing the resensitized receptor”
Background
Naturally Occurring Genetic Variants in the Oxytocin Receptor Alter Receptor Signaling Profiles
Malik, M., Ward, M. D., Fang, Y., Porter, J. R., Zimmerman, M. I., Koelblen, T., Roh, M., Frolova, A. I., Burris, T. P., Bowman, G. R., et al. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.1c00095 · Cited by 17
Functions of the Zinc-Sensing Receptor GPR39 in Regulating Intestinal Health in Animals
Xia, P.-P., Yan, L., Ji, X., Wu, Y., Lian, S.-Q., & Zhu, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012133 · Cited by 14
“In most cases, the first step in weakening the receptor response is mediated by the receptor-specific amino acid phosphorylation of GPCRs by GPCR kinases, especially serine and threonine at the carboxyl terminal of the receptor [35].”
Background
Mapping Structural Determinants within Third Intracellular Loop That Direct Signaling Specificity of Type 1 Corticotropin-releasing Hormone Receptor
Punn, A., Chen, J., Delidaki, M., Tang, J., Liapakis, G., Lehnert, H., Levine, M. A., & Grammatopoulos, D. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.272161 · Cited by 17
β-Arrestin-Based Bret2 Screening Assay for the “Non”-β-Arrestin Binding CB1 Receptor
Vrecl, M., Nørregaard, P. K., Almholt, D. L. C., Elster, L., Pogačnik, A., & Heding, A. (2009) · SLAS DISCOVERY · doi:10.1177/1087057109333101 · Cited by 17
“The V2R C-terminal tail was selected because its role in mediating the formation of stable receptor/β-arr complexes is well established.(17,19) In addition, the V2R has also been successfully used in the β-arrestin-based BRET(2) assay(28) as well as in the Transfluor arrestin recruitment assay.”
Method
Oxytocin and Brain Plasticity
Froemke, R. C., & Carcea, I. (2017) · Principles of Gender-Specific Medicine · doi:10.1016/b978-0-12-803506-1.00037-1 · Cited by 20
Molecular and cellular regulation of neurotensin receptor under acute and chronic agonist stimulation
Souazé, F., & Forgez, P. (2006) · Peptides · doi:10.1016/j.peptides.2006.04.029 · Cited by 17
Maturation of respiratory control in the behaving mammal
Moss, I. R. (2002) · Respiratory Physiology & Neurobiology · doi:10.1016/s1569-9048(02)00070-8 · Cited by 17
Receptor-Mediated Tumor Targeting with Radiopeptides. Part 1. General Concepts and Methods: Applications to Somatostatin Receptor-Expressing Tumors
Eberlé, A. N., Mild, G., & Froidevaux, S. (2004) · Journal of Receptors and Signal Transduction · doi:10.1081/rrs-200040939 · Cited by 17
CK2 Phosphorylation of an Acidic Ser/Thr Di-isoleucine Motif in the Na+/H+ Exchanger NHE5 Isoform Promotes Association with β-Arrestin2 and Endocytosis
Lukashova, V., Szabó, E. Z., Jinadasa, T., Mokhov, A., Litchfield, D. W., & Orlowski, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182881 · Cited by 16
Oxytocin: An Old Hormone, a Novel Psychotropic Drug and its Possible Use in Treating Psychiatric Disorders
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Unveiling the Differences in Signaling and Regulatory Mechanisms between Dopamine D2 and D3 Receptors and Their Impact on Behavioral Sensitization
Kim, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076742 · Cited by 15
“This ability of arrestins to remain associated with class B receptors is facilitated by specific clusters of serine and threonine residues located in the carboxyl-terminal tails of the receptors [66].”
Background
Bivalent ligands promote endosomal trafficking of the dopamine D3 receptor-neurotensin receptor 1 heterodimer
Budzinski, J., Maschauer, S., Kobayashi, H., Couvineau, P., Vogt, H., Gmeiner, P., Roggenhofer, A., Prante, O., Bouvier, M., & Weikert, D. (2021) · Communications Biology · doi:10.1038/s42003-021-02574-4 · Cited by 15
Alterations of ceramide synthesis induce PD-L1 internalization and signaling to regulate tumor metastasis and immunotherapy response
Wofford, W. O., Kim, J., Kim, D., Janneh, A. H., Lee, H. G., Atilgan, F. C., Oleinik, N. V., Kassir, M. F., Saatci, Ö., Chakraborty, P., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114532 · Cited by 15
“24– 26 Sphingolipids play structural roles in regulating the rigidity and shape of the plasma membrane.”
Enhanced Uterine Contractility and Stillbirth in Mice Lacking G Protein-Coupled Receptor Kinase 6 (GRK6): Implications for Oxytocin Receptor Desensitization
Grotegut, C. A., Mao, L., Pierce, S., Swamy, G. K., Heine, R. P., & Murtha, A. P. (2016) · Molecular Endocrinology · doi:10.1210/me.2015-1147 · Cited by 15
Intracellular Trafficking of Gonadotropin Receptors in Health and Disease
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Quantifying the Kinetics of Signaling and Arrestin Recruitment by Nervous System G-Protein Coupled Receptors
Hoare, S. R. J., Tewson, P. H., Sachdev, S., Connor, M. A., Hughes, T. E., & Quinn, A. M. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.814547 · Cited by 15
“The interaction is controlled by the pattern of phosphorylation of the GPCR (the phosphorylation barcode) (Orsini et al., 1999; Oakley et al., 2001; Tobin, 2008; Nobles et al., 2011; Pal et al., 2013; Zhou et al., 2017; Sente et al., 2018; Baidya et al., 2020; DwivediAgnihotri et al., 2020; Latorraca et al., 2020) and…”
Background

Authors: Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., & Caron, M. G.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Caron, Marc G.
ORCID: Oakley, Robert H.
Laporte, Stéphane A.
Barak, Larry S.
Caron, Marc G.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2001-06
Volume: 276
Issue: 22
Pages: 19452-19460
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m101450200
OpenAlex: W2083334427
Cited by: 455
References: 45
Citations by year: 2026: 7 · 2025: 19 · 2024: 8 · 2023: 15 · 2022: 14 · 2021: 13 · 2020: 16 · 2019: 10 · 2018: 11 · 2017: 23 · 2016: 9 · 2015: 9 · 2014: 18 · 2013: 17 · 2012: 19
FWCI: 10.61
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7062 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl061365-04)
National Heart, Lung, and Blood Institute (HL61365)
National Institute of Neurological Disorders and Stroke (NS-19576, R01NS019576)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Keywords: beta-arrestin, G protein-coupled receptors, receptor internalization, receptor desensitization, receptor resensitization, serine/threonine phosphorylation, carboxyl-terminal tail, beta2-adrenergic receptor, oxytocin receptor, angiotensin II type 1a receptor, neurokinin-1 receptor, endocytic vesicles
MeSH terms: beta-Arrestins, beta-Arrestin 2, Amino Acid Sequence, Cell Line, Cell Membrane, Endocytosis, Humans, Luminescent Proteins, Microscopy, Fluorescence, Molecular Sequence Data, Mutation, Phosphorylation, Plasmids, Protein Binding, Receptors, Angiotensin, Receptors, Cell Surface, Recombinant Fusion Proteins, Time Factors, Transfection, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Receptors, Neurotensin, Receptors, Neurokinin-1, Receptors, Oxytocin, Microscopy, Confocal, Arrestins, Receptor, Angiotensin, Type 1, Green Fluorescent Proteins

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Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-β-arrestin complexes after receptor endocytosis

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