RNF138 antibody - C-terminal region (ARP33005_P050)
- Known as:
- RNF138 (anti-) - C-terminal region (ARP33005_P050)
- Catalog number:
- arp33005_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- RNF138 antibody - C-terminal region (ARP33005_P050)
Related genes to: RNF138 antibody - C-terminal region (ARP33005_P050)
- Gene:
- RNF138 NIH gene
- Name:
- ring finger protein 138
- Previous symbol:
- -
- Synonyms:
- STRIN, NARF
- Chromosome:
- 18q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-21
- Date modifiied:
- 2016-04-05
Related products to: RNF138 antibody - C-terminal region (ARP33005_P050)
Related articles to: RNF138 antibody - C-terminal region (ARP33005_P050)
- ADP-ribosylation (ADPr) is a post-translational modification that has regulatory roles in multiple cellular pathways including the DNA damage response and in innate immunity. Recently, it has been uncovered that ADP-ribose can be further modified by a family of ubiquitin E3 ligases, the DELTEXES, which catalyze ubiquitin transfer directly onto ADP-ribose, creating a hybrid ADPr-Ub modification which can be recognized by proteins with dedicated ADPr-Ub binding domains. With this hybrid modification recently been identified in cellular systems, we use a series of in vitro and cellular assays in human cells to investigate the amino acid preference for ADPr-Ub production as well as conditions required for reversal of the modification. We show that ADPr on both serine and glutamate-linked peptides can be ubiquitinated by the RING-DTC domains of DTX2 and DTX3L in vitro and that this can be recognized by RNF114, RNF138 and RNF166 for ubiquitin chain elongation. Finally, we demonstrate that DTX2 rather than DTX3L plays a role in ADPr-Ub production at sites of DNA damage to promote the recruitment of RNF114, RNF138, and RNF166 in an HPF1-independent manner. - Source: PubMed
Publication date: 2026/04/02
Chatrin ChatrinZhu KangSimmons Michael D RMaginn LucySchützenhofer KiraLu YangĐukić NinaWijngaarden SvenKloet Max SKliza Katarzyna WiktoriaHeden van Noort Gerbrand J van derFilippov Dmitri VAhel DraganaSmith RebeccaAhel Ivan - RING-UIM E3 ligases, a subfamily within the RING-type E3 ligases, comprise four members: RNF114, RNF125, RNF138, and RNF166. These ligases are crucial in various biological processes, including immunity, inflammation, epigenetics, and homologous recombination. Extensive research has demonstrated that RING-UIM E3 ligases fulfill specific biological roles in carcinogenesis by ubiquitinating critical oncogenes and tumor suppressors, thereby modulating various signaling pathways, differing their functions across distinct cancer contexts. This review comprehensively examines the multifaceted roles of RING-UIM E3 ligases in human cancers, elucidates the molecular mechanisms underpinning their actions and regulatory effects on cancer cells, and explores their potential clinical applications. - Source: PubMed
Publication date: 2025/10/14
Wang YeZhao YueXin QiZhang Jihong - The ataxia telangiectasia mutated (ATM) kinase orchestrates the early stages of DNA double-strand break repair by promoting hyperphosphorylation of CtIP, a key step in the initiation of DNA end resection. However, the regulatory mechanisms controlling resection extent remain incompletely understood. Here we identify ERCC6L2 as a key regulator of DNA end resection in response to ATM inhibition. ERCC6L2 undergoes liquid-liquid phase separation via its intrinsically disordered regions, forming dynamic nuclear condensates that regulate CtIP stability. Disruption of these condensates renders CtIP susceptible to RNF138-mediated ubiquitination and degradation, thereby mitigating the heightened chromatin recruitment of CtIP induced by ATM inhibition. Intriguingly, ERCC6L2 is frequently downregulated in multiple cancer types and correlates with resistance to ATM inhibitors in both in vitro and in vivo settings. Our findings unveil the crucial role of ERCC6L2-CtIP condensates in governing the extent of DNA end resection and underscore the potential significance of ERCC6L2 as a predictive biomarker for ATM inhibitor response. - Source: PubMed
Publication date: 2025/09/05
Yin YixinLin JinlongCai XiaoxiaNie RuncongLin JiliangLi ShutingXiang ZhichengLing YihongZhang YiyangZhou JieChen JieweiLin WenpingDuan JinlingZheng XueyiXie DanCai Muyan - Myogenesis is a strictly regulated process driven by signaling pathways activating muscle-specific gene expression. During myogenesis, muscle stem cells exhibit DNA damage response (DDR) features, which are essential for myoblast differentiation and skeletal muscle regeneration. However, the specific roles of DDR-associated proteins in these processes are not yet fully understood. Gene knockdown and knockout were used in cell and animal models to study RNF138's function in myoblast differentiation and skeletal muscle regeneration. Multi-omics profiling, including transcriptomics and proteomics, was conducted to identify the key proteins regulated by RNF138 in myogenesis. Protein turnover assays were utilized to investigate RNF138's role in APC protein turnover. Immunofluorescence microscopy was performed to confirm the protein colocalization and subcellular localization. RNF138 expression increases during myoblast differentiation and in regenerating myofibers following muscle injury. Knockdown of RNF138 in C2C12 myoblasts impairs myogenic differentiation and fusion. Additionally, -deficient mice exhibit delayed muscle regeneration following cardiotoxin-induced injury. Multi-omics profiling, including transcriptomics and proteomics, reveals that Wnt/β-catenin signaling, a key driver of myogenic differentiation, is enhanced by RNF138. Mechanistically, RNF138 stabilizes β-catenin and enhances its nuclear localization by facilitating lysosomal degradation of APC, a component of the β-catenin degradation complex responsible for mediating the export of β-catenin from the nucleus to the cytoplasm for further ubiquitin-proteasome degradation. We reveal a noncanonical role for RNF138, an E3 ubiquitin ligase, as a positive regulator of myoblast differentiation and skeletal muscle regeneration via the Wnt/β-catenin pathway. This finding highlights the noncanonical function of RNF138 beyond its known roles in DDR and other cellular processes. Therefore, RNF138 provides a potential link between DDR and myoblast differentiation, offering new insights into the molecular regulation of muscle regeneration. - Source: PubMed
Publication date: 2025/03/18
Wang WenhaoWang ZhuohuaLi RourongHuang WeiyiLing QiaoLi XiaoxiaoLi ZanCao ManqiZhang ZhihuiSun QingrongLiang ZhijuanZhang Hua-AnJiang XuanLin ChuwenChen YaoqingZhao BoZhao YuPan Ji-AnPeng Xiaoxue - Resistance to chemotherapy is a significant concern in the treatment of nasopharyngeal carcinoma (NPC), and occurs due to various mechanisms. This study is aimed to evaluate the effects of RING finger protein 138 (RNF138) in the development of cisplatin resistance to NPC. After gene overexpression and silencing, the expression levels of RNF138 were evaluated. The impacts of RNF138 on the proliferation and apoptosis rate of NPC cells were then assessed. γ-H2AX-mediated DNA damage was determined via immunofluorescence assay. Moreover, a tumor xenograft mouse model was developed to investigate the role of RNF138 on NPC progression in vivo. Additionally, transcriptome analysis was performed in 5-8 F cells transfection with OE-RNF1138 or OE-NC.Cisplatin significantly inhibited the proliferation, and promoted apoptosis and DNA damage in NPC cells; however, overexpression of RNF138 reversed the aforementioned regulatory role of cisplatin on NPC cells. Knockdown of RNF138 resulted in contrasting phenotypic outcomes. Additionally, in nude mice, RNF138 overexpression attenuated the suppressive effects of cisplatin on the growth of xenograft tumor, while RNF138 silencing further enhanced the inhibiting role of cisplatin. We further indicated that in 5-8 F cells following RNF138 overexpression, some pathways such as PI3K-Akt signaling pathway, human papillomavirus infection and ErbB signaling pathway that have been reported to be associated with NPC progression and cisplatin resistance were significantly enriched. These findings indicate that the modulation of RNF138 could potentially address the issue of chemotherapy failure by overcoming cisplatin resistance in NPC cells, making it a promising candidate for targeted drug therapy. - Source: PubMed
Publication date: 2025/01/09
Xu HangyuYin QingFan LinnaZhao YatingSong BiyingXu QifanZhu JieXu Meifen