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Validated All-in-One™ qPCR Primer for ARRB2(NM_004313.4) Search again
Product ID:
HQP149950
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ARB2, ARR2, BARR2
Gene Description:
arrestin beta 2
Target Gene Accession:
NM_004313.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined. [provided by RefSeq].
Gene References into function
- LH/CG R activation is sufficient to expose a conformation in which Asp-564 in the 3i loop confers high affinity binding selectively to arrestin2.
- Phosphorylation of beta-arrestin2 regulates its function in internalization of beta(2)-adrenergic receptors.
- beta-arrestin2 can function not only as a regulator of CXCR4 signaling but also as a mediator of stromal cell-derived factor 1alpha-induced chemotaxis, via the ASK1/p38 MAPK pathway
- role of beta-arrestin, dynamin, and clathrin-dependent pathway in internalization of the complement 5a anaphylatoxin receptor
- this protein functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2.
- examination of desensitization, internalization, and signaling functions demonstrated by RNA interference
- role in angiotensin II activation of extracellular signal-regulated kinases 1 and 2
- endocytosis of Frizzled 4 (Fz4) in human embryonic kidney 293 cells was dependent on added Wnt5A protein and was accomplished by beta-arrestin 2, which was recruited to Fz4 by binding to phosphorylated Dvl2
- findings indicate a physiologically significant, unanticipated role for beta arrestin 2 in regulating TGF-beta signaling through internalization and subsequent decreased signaling of TGF-beta receptors
- results suggest that physiological levels of beta-arrestin1 may act as "dominant-negative" inhibitors of beta-arrestin2-mediated extracellular signal-regulated kinases 1 and 2 activation
- arrestin 2 has a role in activating a MAPK pathway that regulates Nur77, which in turn modulates NK(1)R-mediated nonapoptotic programmed cell death
- Beta-arrestin2 mediates a crosstalk between beta-2 adrenergic receptors and NF-kappaB signaling pathways
- Data show how the ability of receptors such as angiotensin type 1A to interact with beta-arrestin 2 determines both the mechanism of extracellular signal-regulated kinase 1 and 2 activation as well as the physiological consequences of this activation.
- Arrestin2 and arrestin3 in striatal homogenates bind to the third cytoplasmic loop of the D2 receptor.
- Arrestin has a role in regulating MAPK activation and preventing NADPH oxidase-dependent death of cells expressing CXCR2
- protease-activated receptor-2-mediated migration of tumor cells requires both beta-arrestin-1 and -2
- analysis of the glucagon-like peptide-1 receptor beta-arrestin 2 interaction
- beta-Arrestin 2 and GRK2 are potential mediators of signaling by activated Smoothened
- alpha(1a)-ARs recycle rapidly by an agonist-independent, constitutive, beta-arrestin-dependent process and that this can transport "alpha-blockers" into cells carrying these receptors.
- Agonist-controlled association and dissociation of beta-arrestins from prephosphorylated receptors should permit rapid control of receptor sensitivity.
- beta-arrestin 2 can mediate chemotaxis through mechanisms which may be G-protein-independent (Ang II receptors) or -dependent (LPA receptors).
- filamin A, and beta-arrestin form a signaling complex that is destabilized by agonist- or expression-mediated increases in GRK2/3 activity
- ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes
- beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform.
- Role in the activation of the P2X(7) receptor.
- GLP-2 receptor C terminus has a role in modulating beta-arrestin-2 association but not ligand-induced desensitization, endocytosis, and G-protein-dependent effector activation
- MKP7 also binds beta-arrestin 2 via amino acids 394-443 of MKP7, the same region that interacts with JIP-1
- Recruitment of beta-arrestin2 to carboxyl terminal region of beta2AR is important for ERK localization to the nucleus.
- Endogenous beta-arrestin1 functions exclusively in the phosphorylation-dependent receptor internalization, whereas endogenous beta-arrestin2, but not beta-arrestin1, is required for the phosphorylation-independent receptor internalization.
- beta-arrestin2 is identified as a phosphorylation-regulated suppressor of UV induced NF-kappaB activation
- TSH receptor is a member of the class A of G protein-coupled receptors, which have a higher affinity to beta-arrestin 2 than beta-arrestin 1 and do not colocalize with beta-arrestins in endosomes.
- Our results show that PAR1-mediated activation of Src and ERK1/2 in HEK 293 cells was increased with overexpression of beta-arrestin1 or depletion of beta-arrestin2.
- The presence of the alpha(2C)AR within the heterodimer resulted in a marked reduction in the level of GRK2-mediated alpha(2A)AR phosphorylation, which was accompanied by a qualitative attenuation of beta-arrestin recruitment
- RACK1 and beta-arrestin compete to sequester distinct 'pools' of PDE4D5.
- Data show that beta-arrestin2, which typically shows a cytoplasmic localization owing to constitutive nuclear export, appears in the nucleus after stimulation of the G-protein-coupled odorant receptor hOR17-4.
- Results suggest that nephrin Y1193 serves as a molecular switch that determines the integrity of the slit diaphragm by functional competition between beta-arrestin2 and podocin.
- Recombinant human beta-arrestin2 is redistributed into the dendritic knobs of mouse olfactory receptor neurons after treatment with a complex odorant mixture. Prolonged odorant exposure results in accumulation of beta-arrestin2 in intracellular vesicles.
- receptor interaction with beta-arrestin to co-precipitate Src and activate ERK1/2 was obviated by expressing a constitutively active c-SrcY527A mutant, suggesting direct binding of activated Src to PTH1R
- This is the first association analysis of ARRB2, and our results indicate that ARRB2 may play a role in the pathophysiology of METH use disorder.
- Our data suggest that in cirrhosis-induced vasodilation, the AT1-R is desensitized by GRK-2 and beta-arrestin-2 and that changed patterns of phosphorylated Ca(2+) sensitizing proteins decrease Ca(2+) sensitivity.
- results demonstrate the ability of beta-arrestins to recruit diacylglycerol kinases to ligand-activated M1 muscarinic receptors
- Data show that 5-HT(4) receptor stimulation in primary neurons produced a potent but transient activation of the ERK pathway that is dependent on Src tyrosine kinase but totally independent of beta-arrestin.
- endoglin and beta-arrestin2 interact and have roles in regulating transforming growth factor-beta-mediated ERK activation and migration in endothelial cells
- regulates its beta-arrestins selectivity and subsequent receptor internalization and adenylyl cyclase desensitization
- ARRB1 and ARRB2 play an important role in biological processes involved in the regulation of smoking urgency (that is time to smoke first cigarette).
- Evidence was also obtained that the proper clustering of the receptor in these microdomains was important for effective agonist-induced NK1-R signaling and for its interaction with beta-arrestin2.
- identification of a novel polymorphism of the promoter region of the ARRB2 gene in Caucasians and the association with ARRB2 expression
- Mutation of the IP6-binding sites impair oligomerization, reduce interaction with Mdm2, and inhibit p53-dependent antiproliferative effects of beta-arr2
- beta-arrestin2 supported protein kinase C-independent ERK1/2 activation by the AT1a rceptor
- In conclusion, the DRY motif and C-terminal tail of the GPCRs determine complementarily their intracellular trafficking behavior by regulating the affinity to beta-arrestin and G protein coupling.
- A mechanism by which endosomal ECE-1 degrades neuropeptides in endosomes to disrupt the peptide/receptor/beta-arrestin complex, freeing internalized receptors from beta-arrestins and promoting recycling and resensitization, is proposed.
- JNK3 recruits MKK4 to the beta-arrestin-2 scaffold complex by binding to the MAPK docking domain (D-domain) located within the N terminus of MKK4.
- Amino acids important for self-association of beta-arrestin 2 also play an important role in the interaction with both the beta2-adrenoceptor and the ERK1/2 (extracellular-signal-regulated kinase 1/2) MAPKs (mitogen-activated protein kinases).
- using a bioluminescence resonance energy transfer-based biosensor of beta-arrestin 2 and a combination of biased ligands and/or biased mutants of three different 7TMRs, we provide evidence that beta-arrestin can adopt multiple "active" conformations
- beta-arrestin 2, a central element in GPCR trafficking, interacts with and is S-nitrosylated at a single cysteine by endothelial NO synthase (eNOS), and that S-nitrosylation of beta-arrestin 2 is promoted by endogenous S-nitrosogluthathione.
- Agonist-selective, receptor-specific interaction of human P2Y receptors with beta-arrestin-1 and -2.
- These findings demonstrate that physical interaction of CaM with recombinant and native 5-HT(2C) receptors is critical for G protein-independent, arrestin-dependent receptor signaling.
- C terminus distal to residue 381 does not affect the initial interaction between receptor and beta-arrestin, but its last eight amino acids facilitate receptor internalization in concert with beta-arrestin2
- Arrestin 3 but not arrestin 2 is required for internalization of C-C chemokine receptor CCR7 when bound to C-C chemokine ligand CCL19. In contrast, arrestins are not required for internalization of CCR7/CCL21.
- These results show that G(i2) protein is involved in D(2)R-mediated ERK activation but beta-arrestins 1 and 2 are either not involved or play minor role.
- betaarr2 is localized to the centrosome in cycling cells and to the primary cilium in quiescent cells.
- To the best of our knowledge, this is the first study reporting a positive association between the ARRB2 SNP rs1045280 and tardive dyskinesia in schizophrenic patients.
- This study demonstrates that TLR2 signaling mediates the morphine-induced apoptosis, and beta-arrestin 2 is a negative regulator in morphine-induced, TLR2-mediated apoptosis.