Ask about this productRelated genes to: RNF166 antibody
- Gene:
- RNF166 NIH gene
- Name:
- ring finger protein 166
- Previous symbol:
- -
- Synonyms:
- MGC2647, MGC14381
- Chromosome:
- 16q24.2-q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-04
- Date modifiied:
- 2019-03-19
Related products to: RNF166 antibody
Related articles to: RNF166 antibody
- Uridine diphosphate N‑acetylglucosamine (UDP‑GlcNAc) has often been overlooked because its source pathway contributes little to glucose flux. However, through O‑GlcNAcylation, even small fluctuations in UDP‑GlcNAc levels can be amplified to shape immune responses. In this study, we utilized porcine deltacoronavirus (PDCoV), an emerging enteropathogenic coronavirus with zoonotic potential, as a model to investigate the role of UDP-GlcNAc in viral infection. Our findings demonstrate that upon PDCoV infection, host cells increase the synthesis of UDP-GlcNAc, which inhibits viral replication by remodeling metabolic pathways. Mechanistically, O-linked N-acetylglucosamine transferase (OGT) transfers an O-GlcNAc moiety from UDP-GlcNAc to RNF166 at T157, resulting in O-GlcNAcylation. This modification enables RNF166 to ubiquitinate the PDCoV membrane (M) protein at K207, thereby promoting its degradation via the ubiquitin-proteasome pathway. Notably, these effects are common in the host response to porcine coronavirus infections, highlighting the intricate interplay among metabolism, glycosylation, and ubiquitination in immune responses. - Source: PubMed
Publication date: 2026/06/25
Qiu RunhuiZhang YuchengZhou JunweiWang JiananTang WenbingXie XinliangCheng YanDing TongSun PengShi YutingXi CailiZhou YanrongFang LiurongXiao Shaobo - 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 - Ubiquitin (Ub) cooperates with other post-translational modifications to provide a tiered opportunity for protein regulation. Deltex E3 ligases were previously implicated in ubiquitylation of ADP-ribose (ADPr)-containing macromolecules in vitro, generating a noncanonical mono-ADPr-Ub ester (MARUbe). We previously identified mono-ADPr ubiquitylation (MARUbylation) on PARP7 in cells, which was extended with K11-linked polyUb, suggesting an intricately regulated, multilayered post-translational modification. Here, we show that the Deltex DTX2 ubiquitylates ADPr modifications on PARP7 in cells, which depends on PARP7 catalytic activity. We further identify RNF114 as the E3 ligase responsible for K11-linked polyUb extension on sites of PARP7 MARUbylation. Using a chemoenzymatic approach, we developed a fluorescent Ub-ADPr probe and find that RNF114 explicitly recognizes MARUbylated species. We used AlphaFold3 to examine the mechanisms of Ub-ADPr recognition and K11-linked polyUb extension by RNF114. We identify a tandem Di19-UIM module in RNF114 as a MARUbe-binding domain (M-UBD), thus providing a reader function that interfaces with K11-specific writer activity. Finally, we describe a small family of M-UBD-containing E3 ligases that demonstrate preference for Ub-ADPr, which we call MARUbe-Targeted Ligases (M-UTLs). - Source: PubMed
Publication date: 2025/10/02
Lacoursiere Rachel EUpadhyaya KapilKaur Sidhu JasleenRodriguez Siordia IvanBejan Daniel SCohen Michael SPruneda Jonathan N - ADP-ribosylation can occur as mono-ADP-ribose (MAR) or be extended into poly-ADP-ribose (PAR). Tankyrase, a PAR transferase, adds PAR to itself and other proteins targeting them for proteasomal degradation via the PAR-binding E3 ligase RNF146. This degradation can be counteracted by RING-UIM E3 ligases RNF114 and RNF166, although the process is unclear. Here, we identify a mechanism that can regulate the balance between MAR and PAR on tankyrase to control degradation. We show that Deltex E3 ligases DTX2 and DTX3 catalyze monoubiquitylation of tankyrase in cells. This ubiquitylation occurs, not on a (canonical) lysine, but rather on MAR, creating a monoubiquitin-MAR hybrid mark. RNF114 and RNF166 recognize this mark using a unique hybrid reader domain and further diubiquitylate it. This ubiquitylation of MAR, which occurs near the ADP-ribose addition site, prevents PAR formation, antagonizing the action of the PAR-binding E3 ligase RNF146 and stabilizing tankyrase. These findings reveal an interplay between ubiquitin, ADP-ribose, and E3 ligases in cellular signaling. - Source: PubMed
Publication date: 2025/09/03
Perrard JeromeGao KevinRing KatherineSmith Susan