Arrestin beta_2 _ ARRB2
- Known as:
- Arrestin beta_2 _ ARRB2
- Catalog number:
- EB06745
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- Arrestin beta_2 _ ARRB2
Related genes to: Arrestin beta_2 _ ARRB2
- Gene:
- ARRB2 NIH gene
- Name:
- arrestin beta 2
- Previous symbol:
- ARR2
- Synonyms:
- BARR2, DKFZp686L0365
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-10
- Date modifiied:
- 2016-10-05
- Gene:
- KCNAB2 NIH gene
- Name:
- potassium voltage-gated channel subfamily A regulatory beta subunit 2
- Previous symbol:
- -
- Synonyms:
- AKR6A5, KCNA2B, HKvbeta2.1, HKvbeta2.2
- Chromosome:
- 1p36.31
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-13
- Date modifiied:
- 2016-10-05
- Gene:
- PSMB10 NIH gene
- Name:
- proteasome subunit beta 10
- Previous symbol:
- MECL1
- Synonyms:
- LMP10, MGC1665, beta2i
- Chromosome:
- 16q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-07-29
- Date modifiied:
- 2015-08-12
Related products to: Arrestin beta_2 _ ARRB2
Related articles to: Arrestin beta_2 _ ARRB2
- Periodontitis, a common chronic inflammatory disease, causes connective tissue degradation, alveolar bone resorption, and tooth loss. G protein coupled receptor class C group 5 member A (GPRC5A) regulates chronic inflammation in several diseases, but its role in periodontitis remains unclear. This study investigated GPRC5A expression and function in periodontitis. In human tissues, GPRC5A expression was assessed by immunohistochemistry and quantitative real-time PCR (qRT-PCR). In vivo, adeno associated virus (AAV) mediated GPRC5A silencing was applied in a murine periodontitis model. In vitro, mechanistic studies used small interfering RNA (siRNA) knockdown, co-immunoprecipitation (Co-IP), mass spectrometry, and western blot in periodontal ligament cells (PDLCs). GPRC5A was upregulated in inflamed periodontal tissues, and its downregulation reduced alveolar bone loss and periodontitis severity in mice. GPRC5A knockdown suppressed inflammatory cytokine production and NF-κB activation in lipopolysaccharide (LPS) stimulated PDLCs. β-arrestin 2 (ARRB2) expression paralleled GPRC5A changes, and mass spectrometry/Co-IP identified eukaryotic elongation factor 2 (EEF2) as an ARRB2 binding partner. GPRC5A silencing reduced LPS induced ARRB2 expression and EEF2 phosphorylation. These data suggest a possible mechanistic link that GPRC5A downregulation mitigates periodontitis through the ARRB2‑EEF2 pathway, though direct evidence of causality is still needed. - Source: PubMed
Publication date: 2026/06/11
Hu YuhanLiu RunxuanChen XinxiaoShang Lingling - Precise spatiotemporal regulation of parathyroid hormone (PTH) and PTH-related peptide signaling through the parathyroid hormone receptor 1 (PTH1R) is fundamental to skeletal development and metabolic bone remodeling, yet the intracellular mechanisms that fine-tune this signaling remain a central unanswered question. Here, we identify neurofibromin 2 (Nf2) as an essential regulator of PTH1R trafficking and signaling. Conditional knockout of in chondrocytes results in short-limbed dwarfism, disrupted growth plate organization, and suppressed chondrocyte proliferation and hypertrophy, and a paradoxical bone phenotype marked by trabecular hyperproliferation and cortical thinning. Mechanistically, Nf2 binds to the PTH1R C-terminal domain (464-591 aa) to promote selective receptor internalization via β-arrestin2 without altering G protein-coupled receptor kinase-mediated PTH1R phosphorylation. Loss of decouples PTH1R from β-arrestin2-mediated endocytosis, leading to sustained and amplified signaling through the cAMP-CREB-pSOX9 (S181) and VEGF axis. Consequently, -deficient mice exhibited bone changes similar to those induced by the PTH1R agonist abaloparatide. These findings establish Nf2 as a chondrocyte-intrinsic gatekeeper of PTH1R signaling and uncover a cellular mechanism for bone homeostasis by targeting Nf2-mediated β-arrestin2 recruitment. - Source: PubMed
Publication date: 2026/06/10
Liao JunguangHe YiliangZhang ChenyangQian QitaoHuang YupingZhang QiShen PanpanZhou ChenheWu MengruiChen Guiqian - Altered detection and preference for sodium are associated with increased sodium intake, and increased sodium intake is associated with increased risk of hypertension. ATR (angiotensin II type 1 receptor) second-messenger signaling is mediated and modulated by ARRB2 (β-arrestin-2), and both ATR and ARRB2 in the brain influence sodium intake. Here, we examined the hypotheses that ARRB2 influences sodium taste hedonics and that these effects involve ATR. - Source: PubMed
Publication date: 2026/06/01
Grobe Connie CHamilton Autumn JTreesukosol YadaGrobe Justin LSegar Jeffrey LSigmund Curt D - Arrestins regulate G protein-coupled receptor (GPCR) signaling by undergoing large-scale conformational rearrangements, yet the solution-state equilibria that underlie arrestin pre-activation remain poorly defined. While prior studies identified slow conformational exchange at the interdomain interface, these minor states could not be structurally linked to activation because their resonances broaden beyond detection upon receptor binding. Here, we use multinuclear NMR spectroscopy to characterize the intrinsic conformational landscape of full-length, human arrestin-2 in solution. We identify two distinct, pre-existing conformational equilibria that mirror key steps of the receptor-driven activation process. First, a slow exchange process populates a receptor-bound-like, interdomain-twisted conformation at physiological temperatures. In parallel, a faster, globally distributed equilibrium populates a state consistent with C-terminal tail release. Dynamic analyses reveal localized rigidification in the receptor-bound-like minor states despite arrestin's overall flexibility, while backbone relaxation data indicate widespread μs-ms conformational exchange. Together, these results demonstrate that arrestin-2 acts as a preorganized scaffold that intrinsically samples receptor-binding relevant conformations in the absence of binding partners. This provides a solution-state framework for arrestin pre-activation and establishes a dynamic fingerprint for future ligand-dependent studies. - Source: PubMed
Shriver Tucker JKahraman KeremPan MingzheDağ ÇağdaşTonelli MarcoRobson Scott AZiarek Joshua J - Archaic introgression has shaped the modern human immune system, particularly components involved in RNA virus responses. In contrast, its contribution to DNA virus defense remains poorly understood. Here, we investigate the contribution of Neandertal- and Denisovan-introgressed haplotypes to viral load of five common DNA viruses in UK Biobank samples, using genome-wide association summary statistics. We identified 18 genome-wide significant associations, predominantly involving Epstein-Barr virus (EBV) and loci within the Major Histocompatibility Complex, including a Denisovan-like haplotype tightly linked to HLA-A*11:01. Notably, the archaic alleles of these haplotypes showed a directional bias toward increased viral loads. Focusing on two chromosome 17 haplotypes associated with higher EBV load, we identified phenotypic associations with blood cell traits and disease markers, as well as functional effects on immune-relevant genes, including GSDMB, ARRB2, and ALOX15. Allele frequency analysis of one of the chromosome 17 haplotypes revealed signatures of shifting modes of selection, possibly reflecting changes in pathogen landscapes over time. Our results suggest that archaic DNA systematically contributes to DNA virus immunity in modern humans, with effects distinct from previously described RNA virus associations. These findings provide novel evolutionary and functional insights into host-virus interactions and the role of archaic admixture in antiviral defense. - Source: PubMed
Rajpara RutviPolishchuk Sofiia StefaniiaYermakovich DanatDannemann Michael