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Journal articles on the topic '?-arrestin'

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Published: 4 June 2021

Last updated: 25 July 2025

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1

Santini, F., R. B. Penn, A. W. Gagnon, J. L. Benovic, and J. H. Keen. "Selective recruitment of arrestin-3 to clathrin coated pits upon stimulation of G protein-coupled receptors." Journal of Cell Science 113, no. 13 (2000): 2463–70. http://dx.doi.org/10.1242/jcs.113.13.2463.

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Non-visual arrestins (arrestin-2 and arrestin-3) play critical roles in the desensitization and internalization of many G protein-coupled receptors. In vitro experiments have shown that both non-visual arrestins bind with high and approximately comparable affinities to activated, phosphorylated forms of receptors. They also exhibit high affinity binding, again of comparable magnitude, to clathrin. Further, agonist-promoted internalization of many receptors has been found to be stimulated by exogenous over-expression of either arrestin2 or arrestin3. The existence of multiple arrestins raises t

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2

JAHNS, Roland, Franck BORGESE, Sabine LINDENTHAL, Annette STRAUB, René MOTAIS, and Bruno FIÉVET. "Trout red blood cell arrestin (TRCarr), a novel member of the arrestin family: cloning, immunoprecipitation and expression of recombinant TRCarr." Biochemical Journal 316, no. 2 (1996): 497–506. http://dx.doi.org/10.1042/bj3160497.

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Arrestins are cytosolic proteins involved in the desensitization of G-protein-coupled receptors. We report the cloning of trout red blood cell arrestin which shows 76, 82 and 52% identity with bovine β-arrestin1, β-arrestin2 and retinal arrestin respectively. Antibodies were generated against the C-terminus of trout red blood cell arrestin. These antibodies detected arrestin in erythrocyte cytosol and were able to precipitate the native protein. The Na+/H+ antiporter of trout red blood cell is activated by β-adrenergic stimulation and is then desensitized whereas the transmembrane signalling p

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3

Rakib, Ahmed, Taslima Akter Eva, Saad Ahmed Sami, et al. "Beta-Arrestins in the Treatment of Heart Failure Related to Hypertension: A Comprehensive Review." Pharmaceutics 13, no. 6 (2021): 838. http://dx.doi.org/10.3390/pharmaceutics13060838.

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Heart failure (HF) is a complicated clinical syndrome that is considered an increasingly frequent reason for hospitalization, characterized by a complex therapeutic regimen, reduced quality of life, and high morbidity. Long-standing hypertension ultimately paves the way for HF. Recently, there have been improvements in the treatment of hypertension and overall management not limited to only conventional medications, but several novel pathways and their pharmacological alteration are also conducive to the treatment of hypertension. Beta-arrestin (β-arrestin), a protein responsible for beta-adre

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4

Li, Dongjun, and Donna Woulfe. "Arrestin-2 Differentially Regulates PAR4 and P2Y12 Receptor Signaling in Platelets." Blood 112, no. 11 (2008): 110. http://dx.doi.org/10.1182/blood.v112.11.110.110.

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Abstract Arrestins play important roles in the function of G Protein-Coupled Receptors (GPCRs) in many cells, but their roles in platelets remain uncharacterized. While the classical role of arrestins is considered to be the internalization and desensitization of GPCRs, more recent studies suggest that arrestins can serve as molecular scaffolds to recruit phosphatidyl inositol-3 kinases (PI3Ks) to GPCRs and promote PI3K-dependent signaling. Due to the multifunctional role of arrestins, we sought to determine whether arrestins regulate Akt activation in platelets and thrombosis in living animal

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Bhattacharya, Somdatta, Joydeep Paul, Srijan Haldar та Kuntal Pal. "Residue-specific orientation of arrestin in 5-HTR1B (Serotonin Receptor)- βArrestin-1 interaction". Journal of Experimental Biology and Agricultural Sciences 12, № 1 (2024): 138–44. http://dx.doi.org/10.18006/2024.12(1).138.144.

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Physiologically G protein-coupled receptors (GPCRs) are an important class of cell surface proteins capable of sensing the exogenous signals across the cell membrane through G-protein-dependent and independent pathways. Activated GPCRs initiate diverse G-protein-independent signalling through interaction with arrestin. Arrestins comprise a family of four proteins that act as signal regulators of GPCRs. Arrestin specificity and assembly orientation with a particular GPCR depend on the finger loop's residues. Recent cryo-EM structural elucidation of neurotensin receptor-1(NTSR1)-β-arrestin1compl

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6

Morris, Gavin E., Carl P. Nelson, Paul J. Brighton, Nicholas B. Standen, R. A. John Challiss, and Jonathon M. Willets. "Arrestins 2 and 3 differentially regulate ETA and P2Y2 receptor-mediated cell signaling and migration in arterial smooth muscle." American Journal of Physiology-Cell Physiology 302, no. 5 (2012): C723—C734. http://dx.doi.org/10.1152/ajpcell.00202.2011.

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Overstimulation of endothelin type A (ETA) and nucleotide (P2Y) Gαq-coupled receptors in vascular smooth muscle causes vasoconstriction, hypertension, and, eventually, hypertrophy and vascular occlusion. G protein-coupled receptor kinases (GRKs) and arrestin proteins are sequentially recruited by agonist-occupied Gαq-coupled receptors to terminate phospholipase C signaling, preventing prolonged/inappropriate contractile signaling. However, these proteins also play roles in the regulation of several mitogen-activated protein kinase (MAPK) signaling cascades known to be essential for vascular re

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7

Cao, Yubo, Sahil Kumar, Yoon Namkung, Laurence Gagnon, Aaron Cho та Stéphane A. Laporte. "Angiotensin II type 1 receptor variants alter endosomal receptor–β-arrestin complex stability and MAPK activation". Journal of Biological Chemistry 295, № 38 (2020): 13169–80. http://dx.doi.org/10.1074/jbc.ra120.014330.

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The angiotensin II (AngII) type 1 receptor (AT1R), a member of the G protein–coupled receptor (GPCR) family, signals through G proteins and β-arrestins, which act as adaptors to regulate AT1R internalization and mitogen-activated protein kinase (MAPK) ERK1/2 activation. β-arrestin–dependent ERK1/2 regulation is the subject of important studies because its spatiotemporal control remains poorly understood for many GPCRs, including AT1R. To study the link between β-arrestin–dependent trafficking and ERK1/2 signaling, we investigated three naturally occurring AT1R variants that show distinct recep

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8

Zarca, Aurélien, Claudia Perez, Jelle van den Bor та ін. "Differential Involvement of ACKR3 C-Tail in β-Arrestin Recruitment, Trafficking and Internalization". Cells 10, № 3 (2021): 618. http://dx.doi.org/10.3390/cells10030618.

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Background: The atypical chemokine receptor 3 (ACKR3) belongs to the superfamily of G protein-coupled receptors (GPCRs). Unlike classical GPCRs, this receptor does not activate G proteins in most cell types but recruits β-arrestins upon activation. ACKR3 plays an important role in cancer and vascular diseases. As recruitment of β-arrestins is triggered by phosphorylation of the C-terminal tail of GPCRs, we studied the role of different potential phosphorylation sites within the ACKR3 C-tail to further delineate the molecular mechanism of internalization and trafficking of this GPCR. Methods: W

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9

Nakaya, Michio, Satsuki Chikura, Kenji Watari та ін. "Induction of Cardiac Fibrosis by β-Blocker in G Protein-independent and G Protein-coupled Receptor Kinase 5/β-Arrestin2-dependent Signaling Pathways". Journal of Biological Chemistry 287, № 42 (2012): 35669–77. http://dx.doi.org/10.1074/jbc.m112.357871.

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G-protein coupled receptors (GPCRs) have long been known as receptors that activate G protein-dependent cellular signaling pathways. In addition to the G protein-dependent pathways, recent reports have revealed that several ligands called “biased ligands” elicit G protein-independent and β-arrestin-dependent signaling through GPCRs (biased agonism). Several β-blockers are known as biased ligands. All β-blockers inhibit the binding of agonists to the β-adrenergic receptors. In addition to β-blocking action, some β-blockers are reported to induce cellular responses through G protein-independent

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10

Qu, Changxiu, Ji Young Park, Min Woo Yun, et al. "Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade." Proceedings of the National Academy of Sciences 118, no. 37 (2021): e2026491118. http://dx.doi.org/10.1073/pnas.2026491118.

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Arrestins were initially identified for their role in homologous desensitization and internalization of G protein–coupled receptors. Receptor-bound arrestins also initiate signaling by interacting with other signaling proteins. Arrestins scaffold MAPK signaling cascades, MAPK kinase kinase (MAP3K), MAPK kinase (MAP2K), and MAPK. In particular, arrestins facilitate ERK1/2 activation by scaffolding ERK1/2 (MAPK), MEK1 (MAP2K), and Raf (MAPK3). However, the structural mechanism underlying this scaffolding remains unknown. Here, we investigated the mechanism of arrestin-2 scaffolding of cRaf, MEK1

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11

Kumar, P., C. S. Lau, M. Mathur, P. Wang та K. A. DeFea. "Differential effects of β-arrestins on the internalization, desensitization and ERK1/2 activation downstream of protease activated receptor-2". American Journal of Physiology-Cell Physiology 293, № 1 (2007): C346—C357. http://dx.doi.org/10.1152/ajpcell.00010.2007.

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β-Arrestins-1 and 2 are known to play important roles in desensitization of membrane receptors and facilitation of signal transduction pathways. It has been previously shown that β-arrestins are required for signal termination, internalization, and ERK1/2 activation downstream of protease-activated-receptor-2 (PAR-2), but it is unclear whether they are functionally redundant or mediate specific events. Here, we demonstrate that in mouse embryonic fibroblasts (MEFs) from β-arrestin-1/2 knockout mice, Gαq signaling by PAR-2, as measured by mobilization of intracellular Ca2+, is prolonged. Only e

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12

Qian, Hongwei, Luisa Pipolo та Walter G. Thomas. "Association of β-Arrestin 1 with the Type 1A Angiotensin II Receptor Involves Phosphorylation of the Receptor Carboxyl Terminus and Correlates with Receptor Internalization". Molecular Endocrinology 15, № 10 (2001): 1706–19. http://dx.doi.org/10.1210/mend.15.10.0714.

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Abstract Arrestins bind to phosphorylated G protein-coupled receptors and participate in receptor desensitization and endocytosis. Although arrestins traffic with activated type 1 (AT1A) angiotensin II (AngII) receptors, the contribution of arrestins to AT1A receptor internalization is controversial, and the physical association of arrestins with the AT1A receptor has not been established. In this study, by coimmunoprecipitating AT1A receptors and β-arrestin 1, we provide direct evidence for an association between arrestins and the AT1A receptor that was agonist- and time-dependent and conting

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13

Wess, Jürgen. "The Two β-Arrestins Regulate Distinct Metabolic Processes: Studies with Novel Mutant Mouse Models". International Journal of Molecular Sciences 23, № 1 (2022): 495. http://dx.doi.org/10.3390/ijms23010495.

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The two β-arrestins (β-arrestin-1 and -2; alternative names: arrestin-2 and -3, respectively) are well known for their ability to inhibit signaling via G protein-coupled receptors. However, β-arrestins can also act as signaling molecules in their own right. Although the two proteins share a high degree of sequence and structural homology, early studies with cultured cells indicated that β-arrestin-1 and -2 are not functionally redundant. Recently, the in vivo metabolic roles of the two β-arrestins have been studied using mutant mice selectively lacking either β-arrestin-1 or -2 in cell types t

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14

Spillmann, Martin, Larissa Thurner, Nina Romantini, et al. "New Insights into Arrestin Recruitment to GPCRs." International Journal of Molecular Sciences 21, no. 14 (2020): 4949. http://dx.doi.org/10.3390/ijms21144949.

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G protein-coupled receptors (GPCRs) are cellular master regulators that translate extracellular stimuli such as light, small molecules or peptides into a cellular response. Upon ligand binding, they bind intracellular proteins such as G proteins or arrestins, modulating intracellular signaling cascades. Here, we use a protein-fragment complementation approach based on nanoluciferase (split luciferase assay) to assess interaction of all four known human arrestins with four different GPCRs (two class A and two class B receptors) in live cells. Besides directly tagging the 11S split-luciferase su

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15

Li, Dongjun, and Donna S. Woulfe. "Arrestin-2 Regulates Akt Activation by G Protein-Coupled Receptors in Platelets." Blood 108, no. 11 (2006): 1525. http://dx.doi.org/10.1182/blood.v108.11.1525.1525.

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Abstract Arrestins have been shown to play important roles in G Protein-Coupled Receptor (GPCR) function in many cells, but their roles in platelets remain uncharacterized. While the classical role of arrestins is considered to be the internalization and desensitization of GPCRs, more recent studies suggest that arrestins can serve as scaffolds to recruit phosphatidyl inositol-3 kinases (PI3K)s to Gq-coupled receptors and promote PI3K-dependent signaling. Thrombin stimulates the PI3K-dependent activation of Akt in platelets in a Gq-dependent manner. Therefore, we sought to determine whether ar

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16

Wang, Yandao, Jieli Huang, Xi Liu та ін. "β-Arrestin-biased AT1R stimulation promotes extracellular matrix synthesis in renal fibrosis". American Journal of Physiology-Renal Physiology 313, № 1 (2017): F1—F8. http://dx.doi.org/10.1152/ajprenal.00588.2016.

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The renin-angiotensin system plays a critical role in the progression of renal fibrosis. Angiotensin II type 1 receptor (AT1R) belongs to the B family of the G protein-coupled receptor (GPCR) family. β-Arrestins are known as negative regulators of GPCRs. Recently, β-arrestins have been found to regulate multiple intracellular signaling pathways independent of G proteins. In this study we investigated the role of β-arrestins in regulating extracellular matrix (ECM) synthesis in renal fibrosis. The rat kidney fibroblast cell line (NRK-49F) was treated with the β-arrestin biased agonist [1-sar, 4

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17

Golan, Moran, Gabriel Schreiber та Sofia Avissar. "Antidepressant-induced differential ubiquitination of β-arrestins 1 and 2 in mononuclear leucocytes of patients with depression". International Journal of Neuropsychopharmacology 16, № 8 (2013): 1745–54. http://dx.doi.org/10.1017/s1461145713000291.

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Abstract β-Arrestins 1 and 2, cytosolic proteins known to mediate receptor desensitization, endocytosis and G protein-independent signalling, are post-translationally modified by ubiquitination regulating their ability to serve as adaptors and scaffolds. β-Arrestins were suggested to play a role in the pathophysiology of depression and in antidepressant mechanism of action. To determine whether a depressive episode or antidepressant treatment induce significant selective differences in β-arrestin 1 and 2 levels or their ubiquitination patterns in leucocytes of patients with depression, 46 outp

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Vishnivetskiy, Sergey A., Luis E. Gimenez, Derek J. Francis, et al. "Few Residues within an Extensive Binding Interface Drive Receptor Interaction and Determine the Specificity of Arrestin Proteins." Journal of Biological Chemistry 286, no. 27 (2011): 24288–99. http://dx.doi.org/10.1074/jbc.m110.213835.

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Arrestins bind active phosphorylated forms of G protein-coupled receptors, terminating G protein activation, orchestrating receptor trafficking, and redirecting signaling to alternative pathways. Visual arrestin-1 preferentially binds rhodopsin, whereas the two non-visual arrestins interact with hundreds of G protein-coupled receptor subtypes. Here we show that an extensive surface on the concave side of both arrestin-2 domains is involved in receptor binding. We also identified a small number of residues on the receptor binding surface of the N- and C-domains that largely determine the recept

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19

BATTELLE, B.-A., A. W. ANDREWS, K. E. KEMPLER, S. C. EDWARDS, and W. C. SMITH. "Visual arrestin in Limulus is phosphorylated at multiple sites in the light and in the dark." Visual Neuroscience 17, no. 5 (2000): 813–22. http://dx.doi.org/10.1017/s0952523800175145.

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Arrestins participate in the termination of phototransduction in both vertebrates and invertebrates. However, the visual arrestins of invertebrates and vertebrates differ significantly from one another in that the invertebrate visual arrestins become phosphorylated rapidly in response to light while those in the photoreceptors of vertebrates do not. In an effort to understand the functional relevance of arrestin phosphorylation, we examined this process in the photoreceptors of the horseshoe crab Limulus polyphemus. We report that Limulus visual arrestin can be phosphorylated at three sites ne

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Karnam, Preethi C., Sergey A. Vishnivetskiy, and Vsevolod V. Gurevich. "Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors." International Journal of Molecular Sciences 22, no. 22 (2021): 12481. http://dx.doi.org/10.3390/ijms222212481.

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Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the receptor, including inactive phosphorylated and active unphosphorylated. The selectivity of arrestins suggests that they must have two sensors, which detect receptor-attached phosphates and the active receptor conformation independently. Simultaneous engagement of both sensors enables arrestin transition into a high-affinity receptor-binding state. This transition involves a global conformational rea

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Gatto, Federico, Richard A. Feelders, Rob van der Pas та ін. "β-arrestin expression in corticotroph tumor cells is modulated by glucocorticoids". Journal of Endocrinology 245, № 1 (2020): 101–13. http://dx.doi.org/10.1530/joe-19-0311.

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Pituitary-directed medical treatment for Cushing’s disease (CD) is currently represented by membrane receptor targeting drugs (somatostatin analogs and dopamine agonists). Somatostatin and dopamine receptors are regulated by β-arrestins, which have been shown to be differentially regulated by glucocorticoids in non-neuroendocrine cells. In this study we investigated the effects of glucocorticoids on β-arrestin expression in corticotroph tumor cells. First, AtT20 cells, a mouse model of CD, were exposed to dexamethasone (Dex) at different time points and β-arrestin expression was evaluated at m

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Vishnivetskiy, Sergey A., Elizabeth K. Huh, Preethi C. Karnam, Samantha Oviedo, Eugenia V. Gurevich, and Vsevolod V. Gurevich. "The Role of Arrestin-1 Middle Loop in Rhodopsin Binding." International Journal of Molecular Sciences 23, no. 22 (2022): 13887. http://dx.doi.org/10.3390/ijms232213887.

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Arrestins preferentially bind active phosphorylated G protein-coupled receptors (GPCRs). The middle loop, highly conserved in all arrestin subtypes, is localized in the central crest on the GPCR-binding side. Upon receptor binding, it directly interacts with bound GPCR and demonstrates the largest movement of any arrestin element in the structures of the complexes. Comprehensive mutagenesis of the middle loop of rhodopsin-specific arrestin-1 suggests that it primarily serves as a suppressor of binding to non-preferred forms of the receptor. Several mutations in the middle loop increase the bin

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23

Gurevich, Vsevolod V. "Arrestins: A Small Family of Multi-Functional Proteins." International Journal of Molecular Sciences 25, no. 11 (2024): 6284. http://dx.doi.org/10.3390/ijms25116284.

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The first member of the arrestin family, visual arrestin-1, was discovered in the late 1970s. Later, the other three mammalian subtypes were identified and cloned. The first described function was regulation of G protein-coupled receptor (GPCR) signaling: arrestins bind active phosphorylated GPCRs, blocking their coupling to G proteins. It was later discovered that receptor-bound and free arrestins interact with numerous proteins, regulating GPCR trafficking and various signaling pathways, including those that determine cell fate. Arrestins have no enzymatic activity; they function by organizi

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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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Kleist, Andrew B., Shawn Jenjak, Andrija Sente та ін. "Conformational selection guides β-arrestin recruitment at a biased G protein–coupled receptor". Science 377, № 6602 (2022): 222–28. http://dx.doi.org/10.1126/science.abj4922.

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G protein–coupled receptors (GPCRs) recruit β-arrestins to coordinate diverse cellular processes, but the structural dynamics driving this process are poorly understood. Atypical chemokine receptors (ACKRs) are intrinsically biased GPCRs that engage β-arrestins but not G proteins, making them a model system for investigating the structural basis of β-arrestin recruitment. Here, we performed nuclear magnetic resonance (NMR) experiments on 13 CH 3 -ε–methionine–labeled ACKR3, revealing that β-arrestin recruitment is associated with conformational exchange at key regions of the extracellular liga

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Willets, Jonathon M., Craig A. Nash, Richard D. Rainbow, Carl P. Nelson, and R. A. John Challiss. "Defining the roles of arrestin2 and arrestin3 in vasoconstrictor receptor desensitization in hypertension." American Journal of Physiology-Cell Physiology 309, no. 3 (2015): C179—C189. http://dx.doi.org/10.1152/ajpcell.00079.2015.

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Prolonged vasoconstrictor-stimulated phospholipase C activity can induce arterial constriction, hypertension, and smooth muscle hypertrophy/hyperplasia. Arrestin proteins are recruited by agonist-occupied G protein-coupled receptors to terminate signaling and counteract changes in vascular tone. Here we determine whether the development of hypertension affects arrestin expression in resistance arteries and how such changes alter arterial contractile signaling and function. Arrestin2/3 expression was increased in mesenteric arteries of 12-wk-old spontaneously hypertensive rats (SHR) compared wi

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Zbieralski, Kacper, та Donata Wawrzycka. "α-Arrestins and Their Functions: From Yeast to Human Health". International Journal of Molecular Sciences 23, № 9 (2022): 4988. http://dx.doi.org/10.3390/ijms23094988.

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α-Arrestins, also called arrestin-related trafficking adaptors (ARTs), constitute a large family of proteins conserved from yeast to humans. Despite their evolutionary precedence over their extensively studied relatives of the β-arrestin family, α-arrestins have been discovered relatively recently, and thus their properties are mostly unexplored. The predominant function of α-arrestins is the selective identification of membrane proteins for ubiquitination and degradation, which is an important element in maintaining membrane protein homeostasis as well as global cellular metabolisms. Among me

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Liu, Xing, Li Ma, Hao Hong Li та ін. "β-Arrestin–biased signaling mediates memory reconsolidation". Proceedings of the National Academy of Sciences 112, № 14 (2015): 4483–88. http://dx.doi.org/10.1073/pnas.1421758112.

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A long-standing hypothesis posits that a G protein-coupled signaling pathway mediates β-adrenergic nervous system functions, including learning and memory. Here we report that memory retrieval (reactivation) induces the activation of β1-adrenergic β-arrestin signaling in the brain, which stimulates ERK signaling and protein synthesis, leading to postreactivation memory restabilization. β-Arrestin2-deficient mice exhibit impaired memory reconsolidation in object recognition, Morris water maze, and cocaine-conditioned place preference paradigms. Postreactivation blockade of both brain β-adrenerg

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Kim, Kiae, Yeonjin Han, Longhan Duan та Ka Young Chung. "Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins". International Journal of Molecular Sciences 23, № 2 (2022): 1000. http://dx.doi.org/10.3390/ijms23021000.

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β-arrestins were initially identified to desensitize and internalize G-protein-coupled receptors (GPCRs). Receptor-bound β-arrestins also initiate a second wave of signaling by scaffolding mitogen-activated protein kinase (MAPK) signaling components, MAPK kinase kinase, MAPK kinase, and MAPK. In particular, β-arrestins facilitate ERK1/2 or JNK3 activation by scaffolding signal cascade components such as ERK1/2-MEK1-cRaf or JNK3-MKK4/7-ASK1. Understanding the precise molecular and structural mechanisms of β-arrestin-mediated MAPK scaffolding assembly would deepen our understanding of GPCR-media

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Seyedabadi, Mohammad, Mehdi Gharghabi, Eugenia V. Gurevich, and Vsevolod V. Gurevich. "Receptor-Arrestin Interactions: The GPCR Perspective." Biomolecules 11, no. 2 (2021): 218. http://dx.doi.org/10.3390/biom11020218.

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Arrestins are a small family of four proteins in most vertebrates that bind hundreds of different G protein-coupled receptors (GPCRs). Arrestin binding to a GPCR has at least three functions: precluding further receptor coupling to G proteins, facilitating receptor internalization, and initiating distinct arrestin-mediated signaling. The molecular mechanism of arrestin–GPCR interactions has been extensively studied and discussed from the “arrestin perspective”, focusing on the roles of arrestin elements in receptor binding. Here, we discuss this phenomenon from the “receptor perspective”, focu

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Pydi, Sai P., Luiz F. Barella, Lu Zhu, Jaroslawna Meister, Mario Rossi та Jürgen Wess. "β-Arrestins as Important Regulators of Glucose and Energy Homeostasis". Annual Review of Physiology 84, № 1 (2022): 17–40. http://dx.doi.org/10.1146/annurev-physiol-060721-092948.

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β-Arrestin-1 and -2 (also known as arrestin-2 and -3, respectively) are ubiquitously expressed cytoplasmic proteins that dampen signaling through G protein–coupled receptors. However, β-arrestins can also act as signaling molecules in their own right. To investigate the potential metabolic roles of the two β-arrestins in modulating glucose and energy homeostasis, recent studies analyzed mutant mice that lacked or overexpressed β-arrestin-1 and/or -2 in distinct, metabolically important cell types. Metabolic analysis of these mutant mice clearly demonstrated that both β-arrestins play key roles

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Wang, Ping, Puneet Kumar, Chang Wang та Kathryn A. DeFea. "Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110α and β by protease-activated receptor 2 and β-arrestins". Biochemical Journal 408, № 2 (2007): 221–30. http://dx.doi.org/10.1042/bj20070483.

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PAR-2 (protease-activated receptor 2) is a GPCR (G-protein-coupled receptor) that can elicit both G-protein-dependent and -independent signals. We have shown previously that PAR-2 simultaneously promotes Gαq/Ca2+-dependent activation and β-arrestin-1-dependent inhibition of class IA PI3K (phosphoinositide 3-kinase), and we sought to characterize further the role of β-arrestins in the regulation of PI3K activity. Whereas the ability of β-arrestin-1 to inhibit p110α (PI3K catalytic subunit α) has been demonstrated, the role of β-arrestin-2 in PI3K regulation and possible differences in the regul

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Sánchez-Soto, Marta, Noelia M. Boldizsar, Kayla A. Schardien та ін. "G Protein-Coupled Receptor Kinase 2 Selectively Enhances β-Arrestin Recruitment to the D2 Dopamine Receptor through Mechanisms That Are Independent of Receptor Phosphorylation". Biomolecules 13, № 10 (2023): 1552. http://dx.doi.org/10.3390/biom13101552.

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The D2 dopamine receptor (D2R) signals through both G proteins and β-arrestins to regulate important physiological processes, such as movement, reward circuitry, emotion, and cognition. β-arrestins are believed to interact with G protein-coupled receptors (GPCRs) at the phosphorylated C-terminal tail or intracellular loops. GPCR kinases (GRKs) are the primary drivers of GPCR phosphorylation, and for many receptors, receptor phosphorylation is indispensable for β-arrestin recruitment. However, GRK-mediated receptor phosphorylation is not required for β-arrestin recruitment to the D2R, and the r

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Perry-Hauser, Nicole A., Tamer S. Kaoud, Henriette Stoy, et al. "Short Arrestin-3-Derived Peptides Activate JNK3 in Cells." International Journal of Molecular Sciences 23, no. 15 (2022): 8679. http://dx.doi.org/10.3390/ijms23158679.

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Arrestins were first discovered as suppressors of G protein-mediated signaling by G protein-coupled receptors. It was later demonstrated that arrestins also initiate several signaling branches, including mitogen-activated protein kinase cascades. Arrestin-3-dependent activation of the JNK family can be recapitulated with peptide fragments, which are monofunctional elements distilled from this multi-functional arrestin protein. Here, we use maltose-binding protein fusions of arrestin-3-derived peptides to identify arrestin elements that bind kinases of the ASK1-MKK4/7-JNK3 cascade and the short

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Gatto, Federico, Nienke R. Biermasz, Richard A. Feelders, et al. "Low beta-arrestin expression correlates with the responsiveness to long-term somatostatin analog treatment in acromegaly." European Journal of Endocrinology 174, no. 5 (2016): 651–62. http://dx.doi.org/10.1530/eje-15-0391.

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AbstractObjectiveThe high expression of somatostatin receptor subtype 2 (SSTR2 also known as sst2) usually present in growth hormone (GH)-secreting adenomas is the rationale for therapy with somatostatin analogs (SSAs) in acromegaly. Although SSTR2 expression is a good predictor for biochemical response to SSA treatment, we still face tumors resistant to SSAs despite high SSTR2 expression. Recently, beta-arrestins (β-arrestins) have been highlighted as key players in the regulation of SSTR2 function.DesignTo investigate whether β-arrestins might be useful predictors of responsiveness to long-t

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Gatto, Federico, Richard Feelders, Rob van der Pas та ін. "β-Arrestin 1 and 2 and G Protein-Coupled Receptor Kinase 2 Expression in Pituitary Adenomas: Role in the Regulation of Response to Somatostatin Analogue Treatment in Patients With Acromegaly". Endocrinology 154, № 12 (2013): 4715–25. http://dx.doi.org/10.1210/en.2013-1672.

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Recent in vitro studies highlighted G protein-coupled receptor kinase (GRK)2 and β-arrestins as important players in driving somatostatin receptor (SSTR) desensitization and trafficking. Our aim was to characterize GRK2 and β-arrestins expression in different pituitary adenomas and to investigate their potential role in the response to somatostatin analog (SSA) treatment in GH-secreting adenomas (GHomas). We evaluated mRNA expression of multiple SSTRs, GRK2, β-arrestin 1, and β-arrestin 2 in 41 pituitary adenomas (31 GHomas, 6 nonfunctioning [NFPAs], and 4 prolactinomas [PRLomas]). Within the

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Marion, Sébastien, Elodie Kara, Pascale Crepieux та ін. "G protein-coupled receptor kinase 2 and β-arrestins are recruited to FSH receptor in stimulated rat primary Sertoli cells". Journal of Endocrinology 190, № 2 (2006): 341–50. http://dx.doi.org/10.1677/joe.1.06857.

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FSH-receptor (FSH-R) signaling is regulated by agonist-induced desensitization and internalization. It has been shown, in a variety of overexpression systems, that G protein-coupled receptor kinases (GRKs) phosphorylate the activated FSH-R, promote β-arrestin recruitment and ultimately lead to internalization. The accuracy of this mechanism has not yet been demonstrated in cells expressing these different molecules at physiological levels. Using sucrose gradient fractionation, we show that FSH induces the recruitment of the endogenous GRK 2 and β-arrestin 1/2 from the cytoplasm to the plasma m

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Attramadal, H., J. L. Arriza, C. Aoki, et al. "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family." Journal of Biological Chemistry 267, no. 25 (1992): 17882–90. http://dx.doi.org/10.1016/s0021-9258(19)37125-x.

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Becuwe, Michel, Antonio Herrador, Rosine Haguenauer-Tsapis, Olivier Vincent, and Sébastien Léon. "Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family." Biochemistry Research International 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/242764.

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In metazoans, proteins of the arrestin family are key players of G-protein-coupled receptors (GPCRS) signaling and trafficking. Following stimulation, activated receptors are phosphorylated, thus allowing the binding of arrestins and hence an “arrest” of receptor signaling. Arrestins act by uncoupling receptors from G proteins and contribute to the recruitment of endocytic proteins, such as clathrin, to direct receptor trafficking into the endocytic pathway. Arrestins also serve as adaptor proteins by promoting the recruitment of ubiquitin ligases and participate in the agonist-induced ubiquit

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Gurevich, Vsevolod V. "Do arrestin oligomers have specific functions?" Cell Signaling 1, no. 1 (2023): 42–46. http://dx.doi.org/10.46439/signaling.1.009.

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Arrestins are a small family of versatile regulators of cell signaling. Arrestins regulate signaling and trafficking of G protein-coupled receptors, regulate and direct to particular subcellular compartments numerous protein kinases, ubiquitin ligases, etc. Three out of four arrestin subtypes expressed in vertebrates self-associate, each forming oligomers of a distinct size and shape. While the structures of the solution oligomers of arrestin-1, -2, and -3 have been elucidated, no function specific for the oligomeric form of either of these three subtypes has been identified thus far. Consider

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Fessart, Delphine, May Simaan та Stéphane A. Laporte. "c-Src Regulates Clathrin Adapter Protein 2 Interaction with β-Arrestin and the Angiotensin II Type 1 Receptor during Clathrin- Mediated Internalization". Molecular Endocrinology 19, № 2 (2005): 491–503. http://dx.doi.org/10.1210/me.2004-0246.

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Abstract β-Arrestins are multifunctional adapters involved in the internalization and signaling of G protein-coupled receptors (GPCRs). They target receptors to clathrin-coated pits (CCPs) through binding with clathrin and clathrin adapter 2 (AP-2) complex. They also act as transducers of signaling by recruiting c-Src kinase to certain GPCRs. Here we sought to determine whether c-Src regulates the recruitment of AP-2 to β-arrestin and the angiotensin II (Ang II) type 1 receptor (AT1R) during internalization. We show that the agonist stimulation of native AT1R in vascular smooth muscle cells (V

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Grotegut, Chad A., Liping Feng, Lan Mao, R. Phillips Heine, Amy P. Murtha та Howard A. Rockman. "β-Arrestin mediates oxytocin receptor signaling, which regulates uterine contractility and cellular migration". American Journal of Physiology-Endocrinology and Metabolism 300, № 3 (2011): E468—E477. http://dx.doi.org/10.1152/ajpendo.00390.2010.

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Desensitization of the oxytocin receptor (OXTR) in the setting of prolonged oxytocin exposure may lead to dysfunctional labor, which increases the risk for cesarean delivery, and uterine atony, which may result in postpartum hemorrhage. The molecular mechanism for OXTR desensitization is through the agonist-mediated recruitment of the multifunctional protein β-arrestin. In addition to its desensitizing function, β-arrestins have recently been shown to simultaneously activate downstream signaling. We tested whether oxytocin stimulation promotes β-arrestin-mediated OXTR desensitization in vivo a

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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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Neill, Jimmy D., L. Wayne Duck, Lois C. Musgrove та Jeffrey C. Sellers. "Potential Regulatory Roles for G Protein-Coupled Receptor Kinases and β-Arrestins in Gonadotropin-Releasing Hormone Receptor Signaling*". Endocrinology 139, № 4 (1998): 1781–88. http://dx.doi.org/10.1210/endo.139.4.5868.

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Abstract GnRH stimulates gonadotropin secretion, which desensitizes unless the releasing hormone is secreted or administered in a pulsatile fashion. The mechanism of desensitization is unknown, but as the GnRH receptor is G protein coupled, it might involve G protein-coupled receptor kinases (GRKs). Such kinases phosphorylate the intracellular regions of seven-transmembrane receptors, permitting β-arrestin to bind, which prevents the receptor from activating G proteins. Here, we tested the effect of GRKs and β-arrestins on GnRH-induced inositol trisphosphate (IP3) production in COS cells trans

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Van Lith, Lambertus H. C., Julia Oosterom, Andrea Van Elsas та Guido J. R. Zaman. "C5a-Stimulated Recruitment of β-Arrestin2 to the Nonsignaling 7-Transmembrane Decoy Receptor C5L2". Journal of Biomolecular Screening 14, № 9 (2009): 1067–75. http://dx.doi.org/10.1177/1087057109341407.

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C5L2 (or GPR77) is a high-affinity receptor for the complement fragment C5a and its desarginated product, C5a-desArg. Unlike the classical C5a receptor CD88, C5L2 does not couple to intracellular G-protein-signaling pathways but is thought to function as a decoy receptor. The authors show that stimulation of C5L2 with C5a and C5a-desArg induces redistribution of green fluorescent protein—labeled β-arrestin2 to cytoplasmic vesicles. C3a and C3a-desArg were inactive in the β-arrestin translocation assay. Direct interaction of ligand-stimulated C5L2 with β-arrestin was confirmed using a novel β-g

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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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Miranda, Connie Jaqueline, Nicole Fernandez, Nader Kamel, et al. "An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1." Journal of Biological Chemistry 295, no. 19 (2020): 6498–508. http://dx.doi.org/10.1074/jbc.ra120.013043.

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Arrestin-1 is the arrestin family member responsible for inactivation of the G protein–coupled receptor rhodopsin in photoreceptors. Arrestin-1 is also well-known to interact with additional protein partners and to affect other signaling cascades beyond phototransduction. In this study, we investigated one of these alternative arrestin-1 binding partners, the glycolysis enzyme enolase-1, to map the molecular contact sites between these two proteins and investigate how the binding of arrestin-1 affects the catalytic activity of enolase-1. Using fluorescence quench protection of strategically pl

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Gurevich, Vsevolod V., and Eugenia V. Gurevich. "Solo vs Chorus: Monomers and Oligomers of Arrestin Proteins." International Journal of Molecular Sciences 23, no. 13 (2022): 7253. http://dx.doi.org/10.3390/ijms23137253.

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Three out of four subtypes of arrestin proteins expressed in mammals self-associate, each forming oligomers of a distinct kind. Monomers and oligomers have different subcellular localization and distinct biological functions. Here we summarize existing evidence regarding arrestin oligomerization and discuss specific functions of monomeric and oligomeric forms, although too few of the latter are known. The data on arrestins highlight biological importance of oligomerization of signaling proteins. Distinct modes of oligomerization might be an important contributing factor to the functional diffe

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Parameswaran, Narayanan, Babu Gonipeta, Sitaram Parvataneni, Nandakumar Packiriswamy та Deepika Sharma. "β-arrestin-1 negatively regulates inflammatory response to polymicrobial sepsis in mice (110.11)". Journal of Immunology 186, № 1_Supplement (2011): 110.11. http://dx.doi.org/10.4049/jimmunol.186.supp.110.11.

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Abstract β-arrestins are scaffolding proteins that regulate a number of receptor signaling pathways including Toll-like receptors. We recently demonstrated that mice lacking either β-arrestin-1 or β-arrestin-2 are protected from lipopolysaccharide-induced lethality and have a markedly reduced inflammatory response. To assess the role of β-arrestin-1 in a clinically relevant model of sepsis, we subjected wild type and β-arrestin-1 knockout mice to cecal-ligation and puncture (CLP) to mimick septic peritonitis and polymicrobial sepsis. Surprisingly, we found that, mortality of β-arrestin-1 knock

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Morales, Paula, Marta Bruix та M. Angeles Jiménez. "Structural Insights into β-arrestin/CB1 Receptor Interaction: NMR and CD Studies on Model Peptides". International Journal of Molecular Sciences 21, № 21 (2020): 8111. http://dx.doi.org/10.3390/ijms21218111.

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Activation of the cannabinoid CB1 receptor induces different cellular signaling cascades through coupling to different effector proteins (G-proteins and β-arrestins), triggering numerous therapeutic effects. Conformational changes and rearrangements at the intracellular domain of this GPCR receptor that accompany ligand binding dictate the signaling pathways. The GPCR-binding interface for G proteins has been extensively studied, whereas β-arrestin/GPCR complexes are still poorly understood. To gain knowledge in this direction, we designed peptides that mimic the motifs involved in the putativ

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