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β-Arrestin-mediated Receptor Trafficking And Signal Transduction.

S. Shenoy, R. Lefkowitz
Published 2011 · Biology, Medicine

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β-Arrestins function as endocytic adaptors and mediate trafficking of a variety of cell-surface receptors, including seven-transmembrane receptors (7TMRs). In the case of 7TMRs, β-arrestins carry out these tasks while simultaneously inhibiting upstream G-protein-dependent signaling and promoting alternate downstream signaling pathways. The mechanisms by which β-arrestins interact with a continuously expanding ensemble of protein partners and perform their multiple functions including trafficking and signaling are currently being uncovered. Molecular changes at the level of protein conformation as well as post-translational modifications of β-arrestins probably form the basis for their dynamic interactions during receptor trafficking and signaling. It is becoming increasingly evident that β-arrestins, originally discovered as 7TMR adaptor proteins, indeed have much broader and more versatile roles in maintaining cellular homeostasis. In this review paper, we assess the traditional and novel functions of β-arrestins and discuss the molecular attributes that might facilitate multiple interactions in regulating cell signaling and receptor trafficking.
This paper references
10.1016/B978-0-12-571135-7.50009-6
Receptor-mediated uptake of lipoprotein-cholesterol and its utilization for steroid synthesis in the adrenal cortex.
M. Brown (1979)
10.3109/10799898709054990
Deactivation of photoactivated rhodopsin by rhodopsin-kinase and arrestin.
H. Kühn (1987)
10.1016/0006-291X(87)91499-9
Molecular cloning of the S-antigen cDNA from bovine retina.
K. Yamaki (1987)
10.1073/PNAS.84.24.8879
Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein).
J. Benovic (1987)
10.1126/SCIENCE.2163110
beta-Arrestin: a protein that regulates beta-adrenergic receptor function.
M. Lohse (1990)
10.1016/s0021-9258(18)55112-7
Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin.
K. Palczewski (1991)
10.1016/s0021-9258(19)37125-x
Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.
H. Attramadal (1992)
10.1126/science.271.5247.363
Role of β-Arrestin in Mediating Agonist-Promoted G Protein-Coupled Receptor Internalization
S. Ferguson (1996)
10.1074/jbc.271.31.18302
Dynamin and β-Arrestin Reveal Distinct Mechanisms for G Protein-coupled Receptor Internalization*
Jie Zhang (1996)
10.1038/383447A0
β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor
O. Goodman (1996)
10.1074/JBC.272.23.15011
Arrestin/Clathrin Interaction
Jason G. Krupnick (1997)
10.1074/jbc.272.49.31051
Clathrin-mediated Endocytosis of the β-Adrenergic Receptor Is Regulated by Phosphorylation/Dephosphorylation of β-Arrestin1*
F. Lin (1997)
10.1074/jbc.272.46.28849
Agonist-Receptor-Arrestin, an Alternative Ternary Complex with High Agonist Affinity*
V. Gurevich (1997)
10.1146/ANNUREV.BIOCHEM.67.1.425
The Ubiquitin System
A. Hershko (1998)
10.1074/jbc.273.48.31640
β-Arrestins Regulate Mitogenic Signaling and Clathrin-mediated Endocytosis of the Insulin-like Growth Factor I Receptor*
F. Lin (1998)
10.1074/jbc.274.23.15971
Feedback Regulation of β-Arrestin1 Function by Extracellular Signal-regulated Kinases*
F. Lin (1999)
10.1016/S0092-8674(00)80735-7
A Model for Arrestin’s Regulation: The 2.8 Å Crystal Structure of Visual Arrestin
J. Hirsch (1999)
10.1074/jbc.274.45.32248
Association of β-Arrestin with G Protein-coupled Receptors during Clathrin-mediated Endocytosis Dictates the Profile of Receptor Resensitization*
Robert H. Oakley (1999)
10.1074/JBC.M910348199
Differential Affinities of Visual Arrestin, βArrestin1, and βArrestin2 for G Protein-coupled Receptors Delineate Two Major Classes of Receptors*
R. Oakley (2000)
10.1074/jbc.275.1.241
Seven Non-contiguous Intracellular Residues of the Lutropin/Choriogonadotropin Receptor Dictate the Rate of Agonist-induced Internalization and Its Sensitivity to Non-visual Arrestins*
K. Nakamura (2000)
10.1074/jbc.M007159200
An Additional Phosphate-binding Element in Arrestin Molecule
S. A. Vishnivetskiy (2000)
10.1074/jbc.M002581200
The Interaction of β-Arrestin with the AP-2 Adaptor Is Required for the Clustering of β2-Adrenergic Receptor into Clathrin-coated Pits*
S. Laporte (2000)
Cloning and functional characterization of salamander rod and cone arrestins.
W. C. Smith (2000)
10.1083/JCB.148.6.1267
β-Arrestin–Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated Erk1/2
K. Defea (2000)
10.1038/35056591
Ubiquitin and proteasomes: Sumo, ubiquitin's mysterious cousin
S. Müller (2001)
10.1073/PNAS.041608198
beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking.
T. Kohout (2001)
10.1074/JBC.M101450200
Molecular Determinants Underlying the Formation of Stable Intracellular G Protein-coupled Receptor-β-Arrestin Complexes after Receptor Endocytosis*
R. H. Oakley (2001)
10.1074/JBC.C100527200
Agonist-promoted Ubiquitination of the G Protein-coupled Receptor CXCR4 Mediates Lysosomal Sorting*
Adriano Marchese (2001)
10.1126/SCIENCE.1063866
Regulation of Receptor Fate by Ubiquitination of Activated β2-Adrenergic Receptor and β-Arrestin
Sudha K. Shenoy (2001)
10.1016/S0955-0674(00)00190-3
Expanding roles for beta-arrestins as scaffolds and adapters in GPCR signaling and trafficking.
W. E. Miller (2001)
10.1073/pnas.041604898
Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds
L. Luttrell (2001)
10.1016/S0969-2126(01)00644-X
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.
M. Han (2001)
10.1089/154065802761001275
The cellular distribution of fluorescently labeled arrestins provides a robust, sensitive, and universal assay for screening G protein-coupled receptors.
R. H. Oakley (2002)
10.1126/SCIENCE.1074683
Targeting of Cyclic AMP Degradation to β2-Adrenergic Receptors by β-Arrestins
S. Perry (2002)
10.1016/S1359-6446(01)02131-6
Target validation of G-protein coupled receptors.
A. Wise (2002)
10.1021/BI025705N
Phosphorylation of beta-arrestin2 regulates its function in internalization of beta(2)-adrenergic receptors.
Fang-Tsyr Lin (2002)
10.1074/jbc.M201379200
Regulation of Arrestin-3 Phosphorylation by Casein Kinase II*
You-me Kim (2002)
10.1126/SCIENCE.1071550
G Protein Pathways
Susana R. Neves (2002)
10.1146/ANNUREV.CELLBIO.19.110701.154617
Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins.
L. Hicke (2003)
10.1074/jbc.M309450200
The Adaptor Protein β-Arrestin2 Enhances Endocytosis of the Low Density Lipoprotein Receptor*
Jiao-Hui Wu (2003)
10.1074/JBC.M209626200
Trafficking Patterns of β-Arrestin and G Protein-coupled Receptors Determined by the Kinetics of β-Arrestin Deubiquitination*
S. Shenoy (2003)
10.1073/pnas.262789099
Desensitization, internalization, and signaling functions of β-arrestins demonstrated by RNA interference
S. Ahn (2003)
10.1126/SCIENCE.1083195
ß-Arrestin 2 Mediates Endocytosis of Type III TGF-ß Receptor and Down-Regulation of Its Signaling
Wei Chen (2003)
10.1126/SCIENCE.1082808
Dishevelled 2 Recruits ß-Arrestin 2 to Mediate Wnt5A-Stimulated Endocytosis of Frizzled 4
W. Chen (2003)
10.1042/BJ20031820
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.
F. Neuschäfer-Rube (2004)
10.1074/jbc.M308281200
The Role of Phosphorylation in D1 Dopamine Receptor Desensitization
Ok-Jin Kim (2004)
10.1016/J.TIPS.2004.06.006
Historical review: a brief history and personal retrospective of seven-transmembrane receptors.
R. Lefkowitz (2004)
10.1074/jbc.M409785200
Activation-dependent Conformational Changes in β-Arrestin 2*
K. Xiao (2004)
10.1126/SCIENCE.1104135
Activity-Dependent Internalization of Smoothened Mediated by ß-Arrestin 2 and GRK2
W. Chen (2004)
10.1016/J.TIPS.2003.12.008
The molecular acrobatics of arrestin activation.
V. Gurevich (2004)
10.1126/SCIENCE.1104193
ß-Arrestin 2 Regulates Zebrafish Development Through the Hedgehog Signaling Pathway
A. M. Wilbanks (2004)
10.1146/ANNUREV.BIOCHEM.73.011303.074118
Protein modification by SUMO.
E. Johnson (2004)
10.1042/BJ20041745
The sustainability of interactions between the orexin-1 receptor and beta-arrestin-2 is defined by a single C-terminal cluster of hydroxy amino acids and modulates the kinetics of ERK MAPK regulation.
Sandra Milasta (2005)
10.1074/JBC.M501129200
β-Arrestin Is Crucial for Ubiquitination and Down-regulation of the Insulin-like Growth Factor-1 Receptor by Acting as Adaptor for the MDM2 E3 Ligase*
L. Girnita (2005)
10.1038/sj.embor.7400373
Monitoring agonist‐promoted conformational changes of β‐arrestin in living cells by intramolecular BRET
Pascale G. Charest (2005)
10.1074/jbc.M501029200
Functional Dissection of an AP-2 β2 Appendage-binding Sequence within the Autosomal Recessive Hypercholesterolemia Protein*
Sanjay Mishra (2005)
10.1016/j.cell.2005.05.012
An Akt/β-Arrestin 2/PP2A Signaling Complex Mediates Dopaminergic Neurotransmission and Behavior
J. Beaulieu (2005)
10.1042/BJ20040807
Involvement of a cytoplasmic-tail serine cluster in urotensin II receptor internalization.
Christophe D. Proulx (2005)
10.1038/nrm1701
Ubiquitin-binding domains
L. Hicke (2005)
10.1074/jbc.M412418200
Receptor-specific Ubiquitination of β-Arrestin Directs Assembly and Targeting of Seven-transmembrane Receptor Signalosomes*
S. Shenoy (2005)
10.1073/PNAS.0409534102
Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor.
X. Ren (2005)
10.1038/ncb1327
Regulation of Notch signalling by non-visual β-arrestin
Ashim Mukherjee (2005)
10.1073/PNAS.0409532102
Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signaling.
Jihee Kim (2005)
10.1074/jbc.M403674200
Insulin-induced β-Arrestin1 Ser-412 Phosphorylation Is a Mechanism for Desensitization of ERK Activation by Gαi-coupled Receptors*
C. Hupfeld (2005)
10.1126/SCIENCE.1109237
Transduction of Receptor Signals by ß-Arrestins
R. Lefkowitz (2005)
10.1073/PNAS.0407444102
beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform.
E. Szabó (2005)
10.1038/nsmb1103
The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain
Hang Shi (2006)
10.1210/ME.2006-0098
A phosphorylation cluster of five serine and threonine residues in the C-terminus of the follicle-stimulating hormone receptor is important for desensitization but not for beta-arrestin-mediated ERK activation.
E. Kara (2006)
10.1074/jbc.M508074200
A β-Arrestin Binding Determinant Common to the Second Intracellular Loops of Rhodopsin Family G Protein-coupled Receptors*
S. Marion (2006)
10.1128/MCB.00546-06
Smoothened Signal Transduction Is Promoted by G Protein-Coupled Receptor Kinase 2
A. Meloni (2006)
10.1161/01.RES.0000242563.47507.ce
Trafficking of G Protein–Coupled Receptors
M. Drake (2006)
10.1038/sj.emboj.7601351
Mdm2 is involved in the ubiquitination and degradation of G‐protein‐coupled receptor kinase 2
Alicia Salcedo (2006)
10.1016/J.DEVCEL.2006.01.016
Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly.
M. A. Edeling (2006)
10.1016/j.molcel.2006.11.007
New roles for beta-arrestins in cell signaling: not just for seven-transmembrane receptors.
R. Lefkowitz (2006)
10.1172/JCI28164
Nicotine induces cell proliferation by beta-arrestin-mediated activation of Src and Rb-Raf-1 pathways.
P. Dasgupta (2006)
10.1073/pnas.0602587103
β-Arrestin2 mediates nephrin endocytosis and impairs slit diaphragm integrity
I. Quack (2006)
10.1126/SCIENCE.1127085
Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling
D. Mukhopadhyay (2007)
10.1146/ANNUREV.PHYSIOL.69.022405.154712
Regulation of receptor trafficking by GRKs and arrestins.
C. C. Moore (2007)
10.1073/pnas.0704849104
Functional specialization of β-arrestin interactions revealed by proteomic analysis
Kunhong Xiao (2007)
10.1016/J.TIBS.2007.09.010
ESCRTing proteins in the endocytic pathway.
S. Saksena (2007)
10.1146/ANNUREV.PHYSIOL.69.022405.154749
β-Arrestins and Cell Signaling
S. Dewire (2007)
10.1146/ANNUREV.PH.69.013107.100021
Beta-arrestins and cell signaling.
S. Dewire (2007)
10.1074/jbc.M700852200
Ubiquitination of β-Arrestin Links Seven-transmembrane Receptor Endocytosis and ERK Activation*
S. Shenoy (2007)
10.1016/J.TIPS.2007.06.006
β-Arrestin-biased ligands at seven-transmembrane receptors
J. D. Violin (2007)
10.1016/J.MOLMED.2007.06.006
Nephrin--a unique structural and signaling protein of the kidney filter.
J. Patrakka (2007)
10.1038/sj.emboj.7601688
Essential role for β‐arrestin 2 in the regulation of Xenopus convergent extension movements
G. Kim (2007)
10.1126/SCIENCE.1134562
Targeting of Diacylglycerol Degradation to M1 Muscarinic Receptors by ß-Arrestins
C. D. Nelson (2007)
10.1074/jbc.M700090200
N-terminal Tyrosine Modulation of the Endocytic Adaptor Function of the β-Arrestins*
S. Marion (2007)
10.1074/JBC.M611483200
The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2.
Kelly N Nobles (2007)
10.1016/J.TIPS.2007.06.009
Collateral efficacy in drug discovery: taking advantage of the good (allosteric) nature of 7TM receptors.
T. Kenakin (2007)
10.1161/01.RES.0000261939.88744.5a
Seven-Transmembrane Receptors and Ubiquitination
S. Shenoy (2007)
10.1016/j.tim.2008.03.006
Ambient pH gene regulation in fungi: making connections.
M. Peñalva (2008)
10.1111/j.1600-0854.2007.00691.x
Distinct Motifs of Neuropeptide Y Receptors Differentially Regulate Trafficking and Desensitization
Moussa Ouédraogo (2008)
10.1126/science.1157983
β-Arrestin–Mediated Localization of Smoothened to the Primary Cilium
Jeffrey J. Kovacs (2008)
10.1073/pnas.0708862105
Agonist-directed signaling of the serotonin 2A receptor depends on β-arrestin-2 interactions in vivo
Cullen L. Schmid (2008)
10.1146/ANNUREV.PHARMTOX.48.113006.094646
G protein-coupled receptor sorting to endosomes and lysosomes.
A. Marchese (2008)
10.1016/j.cell.2008.09.025
Arrestin-Related Ubiquitin-Ligase Adaptors Regulate Endocytosis and Protein Turnover at the Cell Surface
C. H. Lin (2008)
10.1038/embor.2008.199
Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
E. Nikko (2008)
10.1371/journal.pone.0003728
Targeting of β-Arrestin2 to the Centrosome and Primary Cilium: Role in Cell Proliferation Control
Anahi Mollà-Herman (2008)
10.1074/jbc.M800431200
β-Arrestin Scaffolding of Phosphatidylinositol 4-Phosphate 5-Kinase Iα Promotes Agonist-stimulated Sequestration of the β2-Adrenergic Receptor*
C. D. Nelson (2008)
10.1124/mol.107.038570
Distinct Phosphorylation Sites in the SST2A Somatostatin Receptor Control Internalization, Desensitization, and Arrestin Binding
Q. Liu (2008)
10.1074/jbc.M709668200
Nedd4 Mediates Agonist-dependent Ubiquitination, Lysosomal Targeting, and Degradation of the β2-Adrenergic Receptor*
S. Shenoy (2008)
10.1016/j.molcel.2008.05.024
S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking.
Kentaro Ozawa (2008)
10.1073/pnas.0804246105
Distinct conformational changes in β-arrestin report biased agonism at seven-transmembrane receptors
A. Shukla (2008)
10.1124/mol.108.045948
Arrestin Binds to Different Phosphorylated Regions of the Thyrotropin-Releasing Hormone Receptor with Distinct Functional Consequences
B. Jones (2008)
10.1074/jbc.M710515200
β-Arrestin-mediated Signaling Regulates Protein Synthesis*
Scott M Dewire (2008)
10.1074/jbc.C800061200
β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated Pathway*
R. Lipsky (2008)
10.1074/jbc.M806086200
Dual Role of the β2-Adrenergic Receptor C Terminus for the Binding of β-Arrestin and Receptor Internalization*
C. Krasel (2008)
10.1091/mbc.E08-05-0448
Smoothened signaling in vertebrates is facilitated by a G protein-coupled receptor kinase.
M. Philipp (2008)
10.1111/j.1600-0854.2007.00688.x
Structure of Vps26B and Mapping of its Interaction with the Retromer Protein Complex
B. M. Collins (2008)
10.1016/j.tips.2008.05.006
Location, location, location…site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling
A. Tobin (2008)
10.2174/138920209787847014
The Arrestin Fold: Variations on a Theme
L. Aubry (2009)
10.1021/bi900369c
Arrestin2/clathrin interaction is regulated by key N- and C-terminal regions in arrestin2.
Ronald C Kern (2009)
10.1002/pmic.200800646
Systematic study of protein sumoylation: Development of a site‐specific predictor of SUMOsp 2.0
J. Ren (2009)
10.1074/jbc.M109.023366
Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking*
D. S. Kang (2009)
10.1073/pnas.0900258106
Identification of βArrestin2 as a corepressor of androgen receptor signaling in prostate cancer
V. Lakshmikanthan (2009)
10.1074/jbc.M109.008078
Mdm2 Directs the Ubiquitination of β-Arrestin-sequestered cAMP Phosphodiesterase-4D5*
X. Li (2009)
10.1124/mol.108.050542
An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors
Hongxiang Lan (2009)
10.1073/pnas.0906541106
Endosomes: A legitimate platform for the signaling train
J. E. Murphy (2009)
10.1073/pnas.0904361106
Selective engagement of G protein coupled receptor kinases (GRKs) encodes distinct functions of biased ligands
David A. Zidar (2009)
10.1038/emboj.2009.128
The deubiquitinases USP33 and USP20 coordinate β2 adrenergic receptor recycling and resensitization
Magali Berthouze (2009)
10.1073/pnas.0901083106
β-Arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2
S. Shenoy (2009)
10.1038/emboj.2009.215
β‐arrestin1 phosphorylation by GRK5 regulates G protein‐independent 5‐HT4 receptor signalling
Gaël Barthet (2009)
10.1074/jbc.M900388200
G Protein-coupled Receptor Kinase-mediated Phosphorylation Regulates Post-endocytic Trafficking of the D2 Dopamine Receptor*
Y. Namkung (2009)
10.1016/j.cell.2010.07.041
GPR120 Is an Omega-3 Fatty Acid Receptor Mediating Potent Anti-inflammatory and Insulin-Sensitizing Effects
D. Oh (2010)
10.1073/pnas.1008461107
Global phosphorylation analysis of β-arrestin–mediated signaling downstream of a seven transmembrane receptor (7TMR)
K. Xiao (2010)
10.1111/j.1476-5381.2009.00466.x
β‐arrestins – scaffolds and signalling elements essential for WNT/Frizzled signalling pathways?
G. Schulte (2010)
10.1074/jbc.M110.115089
Nedd4-1 and β-Arrestin-1 Are Key Regulators of Na+/H+ Exchanger 1 Ubiquitylation, Endocytosis, and Function*
A. Simonin (2010)
10.1074/jbc.M109.091173
Site-specific Phosphorylation of CXCR4 Is Dynamically Regulated by Multiple Kinases and Results in Differential Modulation of CXCR4 Signaling*
J. Busillo (2010)
10.1091/mbc.E10-02-0169
Arrestin-2 Interacts with the Endosomal Sorting Complex Required for Transport Machinery to Modulate Endosomal Sorting of CXCR4
R. Malik (2010)
10.1074/jbc.M110.152116
Small Ubiquitin-like Modifier Modification of Arrestin-3 Regulates Receptor Trafficking*
D. Wyatt (2010)
10.1074/jbc.M110.141549
Arresting a Transient Receptor Potential (TRP) Channel
A. Shukla (2010)
10.1038/nrd3024
Teaching old receptors new tricks: biasing seven-transmembrane receptors
S. Rajagopal (2010)
10.1016/j.cellsig.2010.10.004
Beta-arrestins as regulators of signal termination and transduction: how do they determine what to scaffold?
K. Defea (2011)
10.1111/j.1600-0854.2010.01121.x
Role of ubiquitination in endocytic trafficking of G-protein-coupled receptors.
J. Hislop (2011)
10.1016/j.molmed.2010.11.004
Therapeutic potential of β-arrestin- and G protein-biased agonists.
E. Whalen (2011)



This paper is referenced by
10.3390/ijms22105318
Substance P Serves as a Balanced Agonist for MRGPRX2 and a Single Tyrosine Residue Is Required for β-Arrestin Recruitment and Receptor Internalization
C. Chompunud Na Ayudhya (2021)
10.1038/s42003-021-02014-3
G-protein coupled receptor 35 (GPR35) regulates the colonic epithelial cell response to enterotoxigenic Bacteroides fragilis
A. Boleij (2021)
10.1016/j.jsps.2021.04.015
GPCRs: The most promiscuous druggable receptor of the mankind
K. Al-hosaini (2021)
10.1038/s41380-021-01253-4
How changes in dopamine D2 receptor levels alter striatal circuit function and motivation
E. Simpson (2021)
10.1016/j.celrep.2021.109050
Mechanisms of differential desensitization of metabotropic glutamate receptors.
Nohely Abreu (2021)
10.1016/j.isci.2021.102076
The endocytosis of oxidized LDL via the activation of the angiotensin II type 1 receptor
Toshimasa Takahashi (2021)
10.1371/journal.pbio.3001191
Smoothened transduces Hedgehog signals via activity-dependent sequestration of PKA catalytic subunits
Corvin D Arveseth (2021)
10.1021/acs.jproteome.1c00292
Human Multisubunit E3 Ubiquitin Ligase Required for Heterotrimeric G-Protein β-Subunit Ubiquitination and Downstream Signaling.
Brian D Young (2021)
10.1016/j.chembiol.2021.07.004
Ligand-directed bias of G protein signaling at the dopamine D2 receptor.
Ee Von Moo (2021)
10.1126/scisignal.aav0320
Biased ligands at opioid receptors: Current status and future directions
T. Che (2021)
10.1016/B978-0-12-820472-6.00029-3
Pharmacological Target Engagement and Validation
T. Kenakin (2021)
10.1038/s41418-020-00704-9
Opposing functions of β-arrestin 1 and 2 in Parkinson’s disease via microglia inflammation and Nprl3
Yinquan Fang (2021)
10.1007/s43440-021-00240-4
Effects of Gαi2 and Gαz protein knockdown on alpha2A-adrenergic and cannabinoid CB1 receptor regulation of MEK-ERK and FADD pathways in mouse cerebral cortex.
A. Ramos-Miguel (2021)
10.1016/j.bbapap.2021.140603
Dissecting the structural features of β-arrestins as multifunctional proteins.
Yaejin Yun (2021)
10.1038/s41598-021-80974-6
Overexpression of β-Arrestins inhibits proliferation and motility in triple negative breast cancer cells
Saber Yari Bostanabad (2021)
10.1016/j.neulet.2021.135883
Cannabinoid 2 receptors regulate dopamine 2 receptor expression by a beta-arrestin 2 and GRK5-dependent mechanism in neuronal cells
J. M. Franklin (2021)
10.1016/j.lfs.2021.119691
The relation between ACKR4 and CCR7 genes expression and breast cancer metastasis.
M. M. Mohammed (2021)
10.1016/j.tcb.2020.11.011
Membrane Protein Quality Control Mechanisms in the Endo-Lysosome System.
Richa Sardana (2021)
10.3390/cells10010154
GRKs and Epac1 Interaction in Cardiac Remodeling and Heart Failure
Marion Laudette (2021)
10.12703/r/10-15
Recent advances in basic science methodology to evaluate opioid safety profiles and to understand opioid activities
A. Ehrlich (2021)
10.15252/embj.2020107403
ER‐anchored CRTH2 antagonizes collagen biosynthesis and organ fibrosis via binding LARP6
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