Ask about this productRelated genes to: RanGAP1 antibody
- Gene:
- RANGAP1 NIH gene
- Name:
- Ran GTPase activating protein 1
- Previous symbol:
- SD
- Synonyms:
- Fug1, KIAA1835
- Chromosome:
- 22q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-26
- Date modifiied:
- 2016-10-05
Related products to: RanGAP1 antibody
Related articles to: RanGAP1 antibody
- Ran GTPase-activating protein 1 (RanGAP1) is a known regulator of nucleocytoplasmic transport; however, its specific function within innate immunity remains undefined. Here, we show that low RanGAP1 expression correlates with poor survival outcomes in septic patients and demonstrate that RanGAP1 expression and subcellular localization are dynamically regulated in macrophages following lipopolysaccharide (LPS) stimulation. We observed that deletion of RanGAP1 in macrophages exacerbates sepsis progression by using a cecal ligation and puncture (CLP) murine model. Mechanistically, RanGAP1 deficiency significantly impairs macrophage anti-infective functions, including inflammatory cytokine production, pathogen clearance, and antigen processing. These findings highlight RanGAP1 as a central regulator of macrophage immune responses, suggesting that its activity is a critical determinant of septic outcomes. - Source: PubMed
Publication date: 2026/04/27
Mao LinlinLiu GenmingZhang JiahuanZhao QiongzhiZhang XinyiZhang ShengZhang YueBai Xiaochun - Stress granules (SGs) and P-bodies are dynamic compartments in the cytoplasm of eukaryotic cells. SGs assemble in response to stress. The nuclear transport factor RanGAP1 is linked to the pathologies of several human diseases. RanGAP1 concentrates at nuclear pore complexes, but can also associate with cytoplasmic biomolecular condensates. The small molecule pifithrin-µ (PFT-µ) inhibits Hsp70 family members and has potential as a therapeutic agent. PFT-µ triggers SG formation in human cancer cells. This prompted us to evaluate the subcellular localization of RanGAP1 upon exposure to PFT-µ. We show that RanGAP1 accumulates in unique cytoplasmic compartments that do not colocalize with SGs or P-bodies. - Source: PubMed
Publication date: 2026/03/16
Mezzanotte JustinShi JessicaStochaj Ursula - Impaired nucleocytoplasmic transport (NCT) has emerged as a shared pathogenic mechanism in various neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS). Although mutations in the gene encoding superoxide dismutase 1 (SOD1) account for approximately 20% of familial ALS cases, the impact of mutant SOD1 accumulation on the NCT remains unclear. - Source: PubMed
Publication date: 2026/02/14
Argueti-Ostrovsky ShirelLim Su MinArogundade Olubankole ADiaz-Garcia SandraYunisova GulshanMeng AlexHermann AnitaOng KaileeEremenko EkaterinaBravo-Hernandez MarianaDriscoll Shawn PLee Chao-ZongJiang XinStavsky AlexandraBarel ShirShani TomKahn JoyPfaff Samuel LMonsonego AlonMarsala MartinRavits JohnLagier-Tourenne ClotildeIsraelson Adrian - Alternative splicing (AS) is a ubiquitous post-transcriptional regulatory mechanism, that has greatly expanded the transcriptomic and proteomic diversity in vertebrates. While gene regulation of hematopoiesis has been extensively researched in vertebrates, the functions of species- and cell lineage-specific splice variants in vertebrates are largely unknown. Here, we curate transcriptomic data on fetal hematopoietic organ development in six vertebrates and hematopoietic cell differentiation in humans and mice. To identify functional exon-skipping events among thousands of cassette exons in protein-coding genes for a specific differentiation lineage and species, we develop a machine-learning model interrogating 19 features including dynamic expression, protein structure, and evolutionary conservation, and integrate them into a single prediction score, named Functional AS Score (FAScore). Using FAScore, we identify four previously-uncharacterized functional AS events in which deletion of the AS exon leads to defects in erythropoiesis and myelopoiesis. Furthermore, we demonstrate that deletion of exon 15 of TBC1D23 reduces erythropoiesis in mice and zebrafish through elevated binding capacity to RANBP2/RANGAP1 leading to increased SUMOylation level of HDAC1. Collectively, our study presents a valuable tool to identify functional exon skipping (ES) events during hematopoietic lineage commitment, and establishes a research paradigm that can be broadly applied to other biological processes. - Source: PubMed
Publication date: 2026/01/27
Hu XiaoWang JinruiChen LiYang QinTardaguila ManuelMao BinNiu ShenghuiXu ZijieWang GuiHuaZhang DanZhang YatingZhou ZhenLuo JingHe ZhifengLiu DefuTang ChaoSoranzo NicoleLin Jing-WenJia DaChen Lu - 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