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Arrestin

Arrestins are a family of regulatory proteins that play a crucial role in the desensitization of G protein-coupled receptors (GPCRs).
They act as adapters, binding to activated, phosphorylated GPCRs and uncoupling them from their cognate G proteins, thereby terminating the receptor's signaling.
Arrestins also mediate receptor internalization and trafficking, and can serve as scaffolds for the assembly of signaling complexes.
The arrestin family includes four mammalian isoforms: arrestin-1 (visual arrestin), arrestin-2 (β-arrestin1), arrestin-3 (β-arrestin2), and arrestin-4 (cone arrestin).
These proteins are involved in diverse physiological processes, including visual transduction, inflammatory responses, and cardiovascular function.
Understanding the mechanisms of arrestin-mediated GPCR regulation is an active area of research with implications for the development of novel therapeutic strategies targeting this critical signaling pathway.

Most cited protocols related to «Arrestin»

1
Cryosectioning and Immunohistochemistry of Retinal Tissue
Cited 6 times
The eyes were collected at different time points following RD and fixed in 2% paraformaldehyde (Sigma-Aldrich, Dorset, UK) for 2 h at room temperature post-enucleation. The eyes were then washed with PBS and placed in 10%, 20% and 30% sucrose (Sigma-Aldrich, USA) before embedment in OCT (optimal cutting temperature) compound and cryo-sectioned using Leica CM 1900 cryostat (Leica Microsystems, Milton Keynes, UK) at 16 μm thickness. H & E and immunofluorescent staining was performed following published protocols [18 (link), 19 (link)] and antibodies used were listed in Table 1. A negative control, without the primary antibody, was carried out in each staining.

Antibodies used for immunohistochemistry and western blot

AntibodyDilutionCompanyCatalogue number
CD681:300BioRadMCA1957
Cone-arrestin1:1000MilliporeAB15282
GFAP1:200DAKOZ0334
GS1:2000SigmaG2781
IL-331:50R & DAF3626
Donkey anti-goat IgG Alexa Fluor 4881:300Jackson Immunoresearch705–545-147
Donkey anti-rabbit IgG Alexa Fluor 4881:300Jackson Immunoresearch711–585-152
Goat anti-rat IgG Alexa Fluor 5941:300InvitrogenA-11007
Images were acquired using a Nikon C1 Eclipse TE200-U (Nikon, UK) or an Olympus IX51 inverted fluorescent microscope (Olympus, UK) with the same settings for each antibody. Images were processed using Fiji software (provided in the public domain, https://imagej.net/Fiji/). Briefly, the number of CD68+ immune cells, DAPI-labelled nuclei and cone-arrestin+ photoreceptor cells were counted using a multi-point tool in Fiji. The number of rod cells was calculated by subtracting the number of cone-arrestin+ cells from the total DAPI+ cells in the ONL [20 (link)]. Synaptophysin+ areas in the OPL and IPL areas were measured using a free-hand selection tool in Fiji. GFAP quantification was achieved by counting GFAP-positive fibres within the INL layer and post the INL layer of the retina. The data were presented as mean ± standard error of the mean (SEM), normalised to 100 μm of retinal length.
Augustine J., Pavlou S., Ali I., Harkin K., Ozaki E., Campbell M., Stitt A.W., Xu H, & Chen M. (2019). IL-33 deficiency causes persistent inflammation and severe neurodegeneration in retinal detachment. Journal of Neuroinflammation, 16, 251.
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Publication 2019
anti-IgG Antibodies Arrestin Cell Nucleus Cells DAPI Eye Fibrosis Fluorescent Antibody Technique Glial Fibrillary Acidic Protein Goat Immunoglobulins Immunohistochemistry Microscopy paraform Public Domain Rabbits Retina Retinal Cone Sucrose Synaptophysin
2
XFEL Diffraction Imaging of T4L-Rhodopsin-Arrestin Complex
Cited 6 times

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Publication 2017
Arrestin Rhodopsin
3
Simulating Stochastic Receptor Dynamics
Cited 6 times
The stochastic reactions for R*, described in the panels in Figure 1, were simulated using Gillespie’s method [19 ]. We will begin by describing the simplest cases (Figure 1A–C) where just two fates are possible for each state: either phosphorylation or arrestin binding. First, the mean transition rate constants μ(n) and ν(n) were assigned. Then, for each states, two pseudo-random numbers, r1(n) and r2(n), uniformly distributed between zero and unity, were used. The lifetime that the molecule remained in state R*·P(n) was simulated as −ln(r1(n))/{ν(n)+μ(n)}, and the state to which the molecule transitioned was simulated as phosphorylation if r2(n) < ν(n)/{ν(n)+μ(n)} and as arrestin binding otherwise. If a finite flash width was required, the time of photoisomerization was simulated as uniformly distributed over that flash width. These simulations were very fast, and 106 iterations could be performed in ~1 s on a laptop PC. For the three-state R* activity model, simulation of the full version (Figure 1D) would have required more complicated code, so we chose instead to simulate only the truncated linear configuration (Figure 1E), and in this case 106 iterations again took only ~1 s.
Lamb T.D, & Kraft T.W. (2016). Quantitative modeling of the molecular steps underlying shut-off of rhodopsin activity in rod phototransduction. Molecular Vision, 22, 674-696.
Publication 2016
Arrestin Phosphorylation
4
Structural Insights into NTSR1-βarr1 Complex
Cited 5 times
The initial template for NTSR1-βarr1ΔCT was built from the receptor coordinates of NTSR1-NTS8–13 crystal structure (PDB ID: 4GRV) and arrestin coordinates from the V2Rpp-βarr1 structure (PDB ID: 4jQI). The initial coordinates for the NTS8–13 ligand were taken from the NTSR1-NTS8–13 crystal structure (PDB ID: 4GRV). Models were docked into the EM density map using UCSF Chimera 1.14 52 , then refined by several iterations of automated refinement in Phenix interspersed with manual adjustments in Coot 0.8.953 . The NTSR1 C-terminus was built based on the structure of V2Rpp bound to βarr1 (PDB ID: 4JQI). The final model was subjected to global refinement and minimization in real space using phenix.real_space_refine in Phenix 1.1654 . Molprobity 4.5 was used to evaluate model geometry55 (Extended Data Table 1). FSC curves were calculated between the resulting model and the half map used for refinement as well as between the resulting model and the other half map for cross-validation (Extended Data Fig. 6a).
Huang W., Masureel M., Qianhui Q., Janetzko J., Inoue A., Kato H.E., Robertson M.J., Nguyen K.C., Glenn J.S., Skiniotis G, & Kobilka B.K. (2020). Structure of the Neurotensin Receptor 1 in complex with β-arrestin 1. Nature, 579(7798), 303-308.
Publication 2020
Arrestin Chimera Ligands
5
Molecular Dynamics Simulations of M2R-βarr1 Complex
Cited 5 times
Starting from a model of the M2R-βarr1 complex derived from an earlier refinement (model available upon request), the OPM webserver43 (link) was used to orient the structure with respect to the plane of the lipid bilayer. The aligned structure was then prepared further using CHARMM-GUI44 (link) to place the structure in either a membrane bilayer or a MSP1D1–44 nanodisc. In both cases a 3:2 ratio of POPC to POPG was used for the lipid system. The systems were hydrated with TIP3P water and charge neutralized with 150 mM NaCl. Further system preparation was performed in VMD45 (link), where palmitoylation was added to residue Cys457 of the receptor. Serine 488, 493, 494, 495 and threonine 490 and 491 were phosphorylated with dibasic phosphate. The systems were simulated in NAMD46 (link) with the OPLS-AA/M force field47 (link). OPLS-AA parameters for iperoxo and LY2119620 were obtained with the LigParGen server48 (link). OPLS-AA parameters for POPC were taken from49 (link), while POPG parameters were adapted from POPC and the OPLS-AA small molecule set. OPLS-AA/M parameters for phosphorylated serine and threonine were also developed for this work based on existing OPLS-AA parameters for phosphates50 (link). Parameters for palmitoylated cysteine were developed for this work by combining OPLS-AA/M parameters for cysteine with the lipid parameters of Kulig et al. All simulations followed a 2-fs timestep in the NPT ensemble using a Langevin thermostat set at 300K with a dampening coefficient of 1 ps−1 and a Nosé-Hoover Langevin piston barostat set at 1 atm with a period of 50 fs and a decay of 25 fs. Non-bonded interactions were smoothed starting at 10 Å to 12 Å, where long-range interactions were treated with particle mesh Ewald. Systems were minimized for 2000 steps before being slowly heated from 0K to 300K in 20K increments with 0.4 ns of simulation at each increment. During the heating phase, harmonic restraints of 1 kcal/mol/Å2 (link) were applied to all lipid, protein, and small molecule non-hydrogen atoms. The system was then equilibrated with harmonic restraints of 1 kcal/mol/Å2 applied to all non-hydrogen protein atoms for 2 ns, followed by 2 ns of simulation with restraints on only protein C alpha atoms. These restraints were then gradually reduced first to 0.3 kcal/mol/Å2 for 2 ns before being removed completely. This aggregate 12 ns of heating and equilibration and an additional 18 ns of production simulation were discarded from the final calculated quantities. Each system was then simulated for five replicates of up to 200 ns to produce the results used in this work. Trajectories were analyzed with the VMD software45 (link). Interdomain rotation was calculated as described by Latorraca et. al21 (link) using the inactive and active state crystal structures of arrestin (PDB:1CF151 (link) for the inactive structure and PDB:4ZWJ12 (link)) to define the axis of rotation. These structures were chosen as references, as the rhodopsin-arrestin structure was thought to be the closest analogue to our structure; however results were qualitatively similar with other references.
Staus D.P., Hu H., Robertson M.J., Kleinhenz A.L., Wingler L.M., Capel W.D., Latorraca N.R., Lefkowitz R.J, & Skiniotis G. (2020). Structure of the M2 muscarinic receptor-β-arrestin complex in a lipid nanodisc. Nature, 579(7798), 297-302.
Publication 2020
12-nitroxide stearate acetaminophen cysteine Arrestin Cysteine Epistropheus Hydrogen iperoxo Lipid Bilayers Lipids Palmitoylation Phosphates Protein C Proteins Rhodopsin Serine Sodium Chloride Threonine Tissue, Membrane

Most recents protocols related to «Arrestin»

1
Immunohistochemical Analysis of Retinal Proteins

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Publication 2023
Alexa594 alexa fluor 488 Antibodies Arrestin Clone Cells Cryoultramicrotomy DAPI Eye Goat Mice, House Microscopy, Confocal paraform Rabbits Retinal Cone Rhodopsin Serum Sucrose Triton X-100
2
Immunoblot Analysis of Metabolic Proteins
Immunohistochemistry and immunoblot analysis were performed as previously described (48 (link)). In the current study, blots were incubated with LDHA (1:1,000), LDHB (1:1,000), hexokinase 1 (1:1,000), hexokinase 2 (1:1,000), Aldolase C (1:1,000), cone arrestin (1:1,000), pPKM2 (1:1,000), PKM2 (1:1,000), PKM1 (1:1,000), Pde6β (1:1,000), rhodopsin (1:1,000), rod arrestin (1:1,000), M-opsin (1:1,000), PDH (1:1,000) and actin (1:1,000) antibodies (Table S5) overnight at 4° C. The blots were then washed and incubated with HRP-coupled anti-mouse or anti-rabbit secondary antibodies (as appropriate) for 60 min at room temperature. After washing, blots were developed with enhanced SuperSignal West Dura Extended Duration Substrate (Thermo Fisher Scientific, Waltham, MA) and visualized using a Kodak Imager with chemiluminescence capability.
Rajala A., Bhat M.A., Teel K., Gopinadhan Nair G.K., Purcell L, & Rajala R.V. (2023). The function of lactate dehydrogenase A in retinal neurons: implications to retinal degenerative diseases. PNAS Nexus, 2(3), pgad038.
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Publication 2023
Actins Aldolase C Anti-Antibodies Antibodies Arrestin Chemiluminescence Dura Mater Hexokinase Hexokinase II Immunoblotting Immunohistochemistry LDH 5 Mus Rabbits Retinal Cone Rhodopsin Rod Opsins
3
Immunohistochemical Antibody Characterization
Polyclonal LDHA, LDHB, and aldolase C antibodies were purchased from Proteintech (Rosemount, IL). Rabbit polyclonal red/green cone opsin (M-opsin), S-opsin, cone arrestin, actin, and rabbit and mouse secondary antibodies were obtained from Millipore (Billerica, MA). Monoclonal 1D4 rhodopsin antibody was a kind gift from Dr. James F. McGinnis (University of Oklahoma Health Sciences Center). DAPI used for nuclear staining was procured from Invitrogen-Molecular Probes (Carlsbad, CA). Polyclonal pPKM2 (Y105), PKM2, PKM1, PDH, hexokinase 1, and hexokinase 2 antibodies were obtained from Cell Signaling (Danvers, MA). The monoclonal anti-arrestin antibody was a kind gift from Dr. Paul Hargrave (University of Florida, Gainesville). Polyclonal glial fibrillary acidic protein (GFAP) was purchased from Dako (Carpinteria, CA). Monoclonal GS antibody was purchased from Abcam (Cambridge, MA). The monoclonal Pde6β antibody was purchased from Santa Cruz Biotechnology (Dallas, TX).
Rajala A., Bhat M.A., Teel K., Gopinadhan Nair G.K., Purcell L, & Rajala R.V. (2023). The function of lactate dehydrogenase A in retinal neurons: implications to retinal degenerative diseases. PNAS Nexus, 2(3), pgad038.
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Publication 2023
Actins Aldolase C Antibodies Antibodies, Anti-Idiotypic Arrestin Cone Opsins DAPI Glial Fibrillary Acidic Protein Hexokinase Hexokinase II LDH 5 Molecular Probes Monoclonal Antibodies Mus Rabbits Retinal Cone Rhodopsin Rod Opsins
4
Immunofluorescence Staining of Retinal and Testicular Tissues
Immunofluorescence staining was performed per a previously described protocol (Jiang et al., 2016 (link); Liu et al., 2015 (link)). Mice eyecups and testicular tissues were enucleated after sacrifice, rinsed with 1×PBS with connective tissues trimmed, and fixed in 4% paraformaldehyde (PFA) at 4°C overnight. For eyecups, corneas and lens were subsequently removed without disturbing the retina. Posterior eyecups and testicular tissues were then dehydrated in 30% sucrose for 2 hr, embedded in optimal cutting temperature compound, and frozen sectioned at 5 µm. For in vitro assay, NIH3T3 cells were collected at 48 hr post transfection and fixed in 4% PFA at 4°C overnight. Retinal, testicular, and cellular sections were then blocked in 2% normal goat serum and permeabilized with 0.3% Triton X-100 at room temperature for 1 hr. Those sections were further incubated with primary antibodies (Table 5) at 4°C overnight and corresponding fluorescence-conjugated secondary antibodies (dilution: 1:1000; Invitrogen, Carlsbad, CA, USA) at room temperature for 1 hr. Nuclei were counterstained with Hoechst 33342 (Sigma, St. Louis, MO, USA). Retinal images were collected with a Leica TCS SP5 confocal system (Leica, Wetzlar, Germany), testicular images were taken by LSM 800 confocal microscope (Carl Zeiss, Jena, Germany), and cellular cilia and centriole structures were photographed with Leica TCS SP8 super-resolution live cell imaging confocal system (Leica, Wetzlar, Germany). Leica LAS X Life Science Microscope Software (version 3.7.1.21655) was used to measure cilia and centriole length. ImageJ (version 2.0.0-rc-43/1.50e) was used to measure the relative mean fluorescence intensity of cone arrestin and Ift20 at centriole.
Zhu T., Zhang Y., Sheng X., Zhang X., Chen Y., Zhu H., Guo Y., Qi Y., Zhao Y., Zhou Q., Chen X., Guo X, & Zhao C. (2023). Absence of CEP78 causes photoreceptor and sperm flagella impairments in mice and a human individual. eLife, 12, e76157.
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Publication 2023
Antibodies Arrestin Biological Assay Cell Nucleus Cells Centrioles Cilia Connective Tissue Cornea Fluorescence Fluorescent Antibody Technique Freezing Goat HOE 33342 Lens, Crystalline Microscopy Microscopy, Confocal Mus NIH 3T3 Cells paraform Retina Retinal Cone Serum Sucrose Technique, Dilution Testis Tissues Transfection Triton X-100
5
ACKR3 Internalization Measurement by BRET2
Agonist-mediated internalization of ACKR3 was measured by BRET2 between ACKR3_RlucII and rGFP_CAAX (a gift from M. Bouvier, Université de Montréal) as previously described24 (link). Samples were prepared as described for β-arrestin2 recruitment time courses with the exception of the transfected DNA amounts. HEK293 cells were transfected with 42 ng ACKR3_RlucII and 170 ng rGFP_CAAX DNA, with empty pcDNA3.1 to bring the total DNA amount to 2.5 µg/well. Data presented in Figs. 1, 3, and 4C were collected with a PerkinElmer Victor Luminometer, while the time courses in Fig. 4D and 7 were measured on a Tecan Spark luminometer. All settings were identical to those used for arrestin association (described above). Data is presented as percent change compared to mock treated wells and are a composite of three independent experiments. The percent changes after 30 min were compared for statistical analysis.
Schafer C.T., Chen Q., Tesmer J.J, & Handel T.M. (2023). Atypical Chemokine Receptor 3 ‘Senses’ CXC Chemokine Receptor 4 Activation Through GPCR Kinase Phosphorylation. bioRxiv.
Publication Preprint 2023
Arrestin beta-Arrestin 1 CXCR7 protein, human HEK293 Cells

Top products related to «Arrestin»

1
Ab15282 by Merck Group
Sourced in United States, Germany
AB15282 is a laboratory equipment product. It is a device used for scientific analysis and experimentation. The core function of this equipment is to facilitate the measurement and investigation of various samples and materials in a controlled laboratory environment.
2
Cone arrestin by Merck Group
Sourced in United States, Germany
Cone arrestin is a lab equipment product used in scientific research. It functions as a regulatory protein that interacts with and regulates the activity of cone photoreceptor cells in the retina.
3
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
4
Alexa fluor 488 by Thermo Fisher Scientific
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Alexa Fluor 488 is a fluorescent dye used in various biotechnological applications. It has an excitation maximum at 495 nm and an emission maximum at 519 nm, producing a green fluorescent signal. Alexa Fluor 488 is known for its brightness, photostability, and pH-insensitivity, making it a popular choice for labeling biomolecules in biological research.
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4 6 diamidino 2 phenylindole (dapi) by Merck Group
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DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.
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Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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Mouse monoclonal anti cre antibody by Abcam
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8
4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
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DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.
9
Dapi stain by Thermo Fisher Scientific
Sourced in United States
DAPI (4',6-diamidino-2-phenylindole) is a fluorescent stain that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used in fluorescence microscopy to visualize and locate the nucleus of cells.
10
Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.

More about "Arrestin"

Arrestins are a crucial family of regulatory proteins that play a pivotal role in the desensitization of G protein-coupled receptors (GPCRs).
These adaptor molecules bind to activated, phosphorylated GPCRs, uncoupling them from their cognate G proteins and terminating the receptor's signaling.
The arrestin family encompasses four mammalian isoforms: arrestin-1 (visual arrestin), arrestin-2 (β-arrestin1), arrestin-3 (β-arrestin2), and arrestin-4 (cone arrestin).
These proteins are involved in diverse physiological processes, such as visual transduction, inflammatory responses, and cardiovascular function.
Arrestin research is an active and thriving field with significant implications for the development of novel therapeutic strategies.
PubCompare.ai, an innovative AI-powered platform, can revolutionize your Arrestin research by helping you locate the best protocols from literature, pre-prints, and patents.
This tool utilizes AI-driven comparisons to ensure maximum reproducibility and accuracy, streamlining your research process and unlocking new insights.
In your Arrestin research, you may encounter various tools and techniques, such as Lipofectamine 2000 for transfection, Alexa Fluor 488 for fluorescent labeling, DAPI for nuclear staining, and FBS for cell culture.
Additionally, you may use antibodies like the Mouse monoclonal anti-Cre antibody and stains such as DAPI to visualize and analyze your samples.
Penicillin/streptomycin is a common antibiotic combination used to prevent bacterial contamination in cell culture experiments.
Understanding the mechanisms of arrestin-mediated GPCR regulation is crucial, and PubCompare.ai can be a valuable resource in your Arrestin research journey.
Discover new insights, streamline your workflow, and unlock the full potential of your Arrestin studies with this innovative AI-powered platform.