RNF38 Pre-design Chimera RNAi
- Known as:
- RNF38 Pre-design Chimera RNAi
- Catalog number:
- H00152006-R02
- Product Quantity:
- 10 nmol
- Category:
- -
- Supplier:
- Abno
- Gene target:
- RNF38 Pre-design Chimera RNAi
Related genes to: RNF38 Pre-design Chimera RNAi
- Gene:
- RNF38 NIH gene
- Name:
- ring finger protein 38
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 9p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-23
- Date modifiied:
- 2016-10-05
Related products to: RNF38 Pre-design Chimera RNAi
Related articles to: RNF38 Pre-design Chimera RNAi
- RING E3 ubiquitin (UB) ligases rely on signature RING domains for mediating UB transfer to substrate proteins. The large number of RING E3s and their weak association with substrates pose a significant challenge in identifying the substrates of individual E3s, thereby hindering the elucidation of their biological functions. Here, we utilized phage display to engineer an "orthogonal UB transfer" (OUT) cascade with RING E3 RNF38, enabling the exclusive transfer of an engineered UB (xUB) to its substrates in the cell. The OUT screen revealed RNF38 substrates regulating nucleocytoplasmic transport (Ran, RanGAP1, and KPNA2), protein translation (HuR and Rack1), and endosomal sorting (VPS35). Furthermore, RNF38-catalyzed ubiquitination was found to induce the degradation of the substrate proteins and negatively affect the translocation of transcription factors E2F1 and phosphorylated STAT3 (p-STAT3) into the nucleus. Phage selection of the RNF38 RING library also revealed hotspot residues for E2 interaction, which may guide the engineering of orthogonal E2-E3 pairs with other RING E3s. Overall, our work discovered new roles of RNF38 in regulating nuclear transport and established an anchoring point for expanding OUT cascades within the large family of RING E3s for revealing their UB transfer targets and cellular functions. - Source: PubMed
Publication date: 2026/01/23
Zhou LiJeong In HoLi HangRios NicolasZhang JingWang XiaoyuLiu ShuXie YayunWei WeiJeong Geon HDuong DucSeyfried Nicholas TXue BingzhongShi HangMabb Angela MWang YiyangKiyokawa HiroakiYin Jun - RING family ubiquitin ligases (E3s) employ the RING domain to recruit the E2 thioester ubiquitin (E2∼Ub) intermediate to catalyze the transfer of ubiquitin (Ub) to substrates. A cationic Arg linchpin (LP) residue in the RING domain plays a key role in stabilizing the interface with E2∼Ub, but the identity of the LP residue varies across E3s. Here, we investigate how the LP residue contributes to ubiquitination. Using the model RNF38 system, we demonstrate that substitution of LP to the other 19 available amino acids modulates ubiquitination, ranging from minor reduction to complete abolition. The identity of the LP residue influences E2∼Ub binding but does not correlate with E3 activity. NMR and X-ray crystallography analyses reveal that RNF38 LP variants stabilize E2∼Ub in a catalytically competent conformation to varying degrees. By altering the LP residue in XIAP, we show that the XIAP variant promotes E2∼Ub stabilization and enhances substrate ubiquitination in cells. Our work demonstrates the importance of the LP residue in modulating E2∼Ub conformation to control ubiquitination. - Source: PubMed
Publication date: 2025/08/05
Nakasone Mark ABuetow LoriGabrielsen MadsAhmed Syed FMajorek Karolina ASibbet Gary JSmith Brian OHuang Danny T - Globally, HCC is still one of the most common cancers. N6-methyladenosine (mA) modifications and long-stranded noncoding RNAs (lncRNAs) play key roles in regulating HCC progression. The role of the lncRNA RNF144A-AS1, a newly identified lncRNA, in HCC is unclear. - Source: PubMed
Publication date: 2025/07/29
Kong MinyuLi WendongLi HaoJing YifanXu MinHe YutingGuo Wenzhi - Gilteritinib is a commonly used targeted drug for acute myeloid leukemia (AML), but the emergence of gilteritinib resistance greatly reduces the therapeutic effect. RING finger protein 38 (RNF38), a protein with RING Finger domain and E3 ubiquitin ligase activity, has been implicated in tumorigenesis and drug resistance. However, the role and mechanism of RNF38 in the gilteritinib resistance of AML remains unclear. - Source: PubMed
Publication date: 2024/11/28
Pan YiyunZeng WenLiang TingNie XiaomingLiu KangChen HailongLuo NengpingZhu XiaodanTian KeqiangChen Yijian - To analyze the effect of Linc00511 on thyroid cancer through the miR-4739/RNF38 pathway. - Source: PubMed
Publication date: 2024/05/03
Liu YingHe LeiShi JihongJiang XiaZhang JianxinFeng YongLiu Wei