ARIH1 _ HHARI Antibody
- Known as:
- ARIH1 _ HHARI Antibody
- Catalog number:
- AF1100a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ARIH1 _ HHARI Antibody
Related genes to: ARIH1 _ HHARI Antibody
- Gene:
- ARIH1 NIH gene
- Name:
- ariadne RBR E3 ubiquitin protein ligase 1
- Previous symbol:
- -
- Synonyms:
- HARI, HHARI, UBCH7BP, ARI
- Chromosome:
- 15q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-08-24
- Date modifiied:
- 2016-10-05
Related products to: ARIH1 _ HHARI Antibody
Related articles to: ARIH1 _ HHARI Antibody
- In PINK1 (PTEN induced kinase 1)/PRKN (Parkin)-mediated mitophagy, the rupture of the outer mitochondrial membrane (OMM) emerges as a crucial event required for efficient mitochondrial clearance. Mechanistically, OMM rupture exposes inner mitochondrial membrane (IMM) mitophagy receptors, facilitating subsequent autophagic removal. Despite the important role of OMM rupture in mitophagy, the underlying mechanism remains elusive and technically difficult to monitor. In a recent study, we developed a novel fluorescent biosensor to directly visualize OMM rupture. This technique enables temporal and spatial characterization of OMM rupture and provides a powerful platform to dissect the underlying mechanism. Using this tool, we revealed that VCP (valosin containing protein) and its recruitment factors are required for OMM rupture, suggesting that VCP-dependent remodeling of the OMM proteome primes the rupture of OMM during mitophagy. : ARIH1, Ariadne RBR E3 ubiquitin protein Ligase 1; AMFR, autocrine motility factor receptor; ANKRD13A, ankyrin repeat domain-containing protein 13 A; FUNDC1, FUN14 domain containing 1; OA, oligomycin and antimycin; CID, chemical-induced dimerization; IMM, nner mitochondrial membrane; LC3, microtubule-associated protein 1 light chain 3; MUL1, mitochondrial E3 ubiquitin protein ligase 1; NIX, BCL2 interacting protein 3 like; OMM, outer mitochondrial membrane; UBXN1, ubiquitin regulatory X domain-containing protein 1; UBXN6, ubiquitin regulatory X domain-containing protein 6; VCP, valosin-containing protein; WIPI2, WD repeat domain phosphoinositide interacting protein 2. - Source: PubMed
Publication date: 2026/02/13
Chu Wei-HuaChiang Wei-Chung - Disrupted proteostasis causes various degenerative diseases, and organelle homeostasis is therefore maintained by elaborate mechanisms. Endoplasmic reticulum (ER) stress-induced preemptive quality control (ERpQC) counteracts stress by reducing ER load through inhibiting the translocation of newly synthesized proteins into the ER for their rapid degradation in the cytoplasm. Here, we show that Sec61β, a translocon component, prevents the overproduction of ERpQC substrates, allowing for their efficient degradation by the proteasome. Sec61β inhibits the binding of translation initiation factor eIF4E to the mRNA 5' cap structure by recruiting E3 ligase ARIH1 and eIF4E-homologous protein 4EHP, resulting in selective translational repression of ERpQC substrates. Sec61β deficiency causes overproduction of ERpQC substrates and reduces proteasome activity, leading to cytoplasmic aggresome formation. We also show that Sec61β deficiency causes motor dysfunction in zebrafish, which is restored by exogenous ARIH1 expression. Collectively, translational repression of ERpQC substrates by the Sec61β-ARIH1 complex contributes to maintain ER and cytoplasmic proteostasis. - Source: PubMed
Publication date: 2026/01/27
Kadowaki HisaeHatta TomohisaSugiyama KazumaFukaya TomohiroFujisawa TakaoHamano TakashiMurao NaoyaTakami YasunariMitoma ShuyaNatsume TohruSato KatsuakiHirata HiromiUechi TamayoNishitoh Hideki - E3 ligases partner with E2 enzymes to regulate vast eukaryotic biology. The hierarchical nature of these pairings, with >600 E3s and ~40 E2s in humans, necessitates that E2s cofunction with numerous different E3s. Here, focusing on E3s in the RING-between-RING (RBR) family and their partner UBE2L3 and UBE2D-family E2s, we report an approach to interrogate selected pathways. We screened phage-displayed libraries of structure-based E2 variants (E2Vs) to discover enzymes with enhanced affinity and specificity toward half of all RBR E3 ligases (ARIH1, ARIH2, ANKIB1, CUL9, HOIL1, HOIP, and RNF14). Collectively, these E2Vs allowed distinguishing actions of different cofunctioning E3s, obtaining high-resolution cryogenic Electron Microscopy (cryo-EM) structures of an RBR E3 in the context of a substrate-bound multiprotein complex, and profiling an endogenous RBR E3 response to an extracellular stimulus. Overall, we anticipate that E2V technology will be a generalizable tool to enable in-depth mechanistic and structural analysis of E3 ligase functions, and mapping their activity states and protein partners in cellular signaling cascades. - Source: PubMed
Publication date: 2026/01/02
Du JialeAndree Gisele AHorn-Ghetko DanielStier LucaSingh JaspalKostrhon SebastianKiss LeoMann MatthiasSidhu Sachdev SSchulman Brenda A - - Source: PubMed
Publication date: 2025/11/14
Zhang ZiyiHe ZhaozhaoHuang BoyuCai RuiLi FengnaYin YulongPang Weijun - Non-small cell lung cancer (NSCLC), accounting for the majority of lung cancer, is the leading cause of cancer death worldwide, and molecular targeted drugs promote greatly advance in the treatment of this disease. Overexpression of human epidermal growth factor receptor 2 (HER2) occurs in 1-5% of NSCLC cases, correlating with poorer outcomes and lack of approved targeted drugs. Pyrotinib is an irreversible HER2 receptor tyrosine kinase inhibitor developed for the treatment of HER2-positive advanced solid tumors; however, the comprehensive exploration of Pyrotinib's anti-tumor mechanism in HER2-positive NSCLC cells needs further explored. - Source: PubMed
Publication date: 2025/10/22
Li XiyueWang JiehongLi ShuFang JingHao YueXu ChunweiShu YouShu HongChen JiaojiaoLu NaiyanZhu XueWang KeWang Xun