DDX46 antibody - C-terminal region (ARP37717_T100)
- Known as:
- DDX46 (anti-) - C-terminal region (ARP37717_T100)
- Catalog number:
- arp37717_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- DDX46 antibody - C-terminal region (ARP37717_T100)
Related genes to: DDX46 antibody - C-terminal region (ARP37717_T100)
- Gene:
- DDX46 NIH gene
- Name:
- DEAD-box helicase 46
- Previous symbol:
- -
- Synonyms:
- KIAA0801, FLJ25329, PRPF5, Prp5
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-13
- Date modifiied:
- 2016-01-07
Related products to: DDX46 antibody - C-terminal region (ARP37717_T100)
Related articles to: DDX46 antibody - C-terminal region (ARP37717_T100)
- The DEAD-box proteins of the superfamily II (SF2) RNA/DNA helicases are typically found to be ATP-dependent RNA binding proteins and RNA-dependent ATPases; however, they have poor, nonprocessive, RNA unwinding activity. Moreover, cells contain multiple variants that are associated with specific cellular processes, and they are generally not interchangeable. Thus, they can be thought of as ATP-dependent switches to control the progression and directionality of cellular metabolism and catabolism. We have characterized a DEAD-box protein (LINF08) from the trypanosomatid parasite Leishmania infantum that has homology to the spliceosome protein DDX46/Prp5. It is expressed in the nucleus of the flagellated promastigotes and the immobile axenic amastigotes. It has very high intrinsic ATPase activity that is independent of added nucleic acids, and it is activated both by the usual bound magnesium cation and by calcium, which is a cation that typically does not directly participate in catalysis. DDX46/Prp5 in other eukaryotes is involved in the early proofreading steps of spliceosome assembly to resolve structural aberrations between the U2 small nuclear RNA (snRNA) and the splice junction. Although trypanosomes typically lack introns, all of the mRNAs are transcribed as polycistronic RNAs that are processed into individual mRNAs involving a process known as SL-dependent trans splicing. Trypanosomes retain the spliceosome machinery but the snRNAs are in an abbreviated form. Thus, although LINF08 appears to be a DDX46/Prp5 homolog, it has probably evolved for the unusual splicing machinery and highly variable environment of the parasite. - Source: PubMed
Publication date: 2026/08/14
Abdelkrim Yosser ZinaMokdadi MolkaBanroques JosetteHuvelle EmmelineCrobu LucienSterkers YvonBarhoumi MouradGuizani IkramTanner N Kyle - Snoring-related vibrations have been proposed as a pathogenic factor contributing to upper airway muscle dysfunction in patients with obstructive sleep apnea (OSA). To investigate whether exposure to snoring vibration is linked to muscle weakness, we used an in vitro vibration model to examine its effects on mitochondrial homeostasis in L6 muscle cells at 8, 12, 24, and 48 h. The findings were then compared with mitochondrial alterations in the upper airway muscles from snorers and patients with OSA. Proteomic analysis of L6 myoblasts revealed extensive remodeling of the mitochondrial proteome at 8 h, affecting pathways involved in oxidative phosphorylation, protein import, ribosome biogenesis, and RNA processing. Respiratory chain remodeling was subunit-specific, with increased abundance of selected components of Complexes I, IV, and V, including NDUFS4, COX5A, and ATP5PD. However, reductions in spliceosome-associated factors, such as SRSF2 and DDX46, along with alterations in mitochondrial ribosomal proteins, indicated impaired RNA processing and protein synthesis. Furthermore, both proteomic and transcriptomic analyses revealed activation of a mechanosensing-mechanotransduction axis, with early upregulation of integrin subunits and mechanosensitive ion channels, followed by transient activation of focal adhesion signaling. Despite transcriptional upregulation of selected Complex IV subunits Cox5a and Cox6a2, this response was accompanied by accumulation of unspliced pre-mRNA, indicating impaired RNA processing efficiency and a decoupling between transcript and protein levels. Real-time Seahorse assay revealed a collapse of mitochondrial respiration and glycolytic reserve at 8 h. Although mitochondrial oxygen consumption recovered after 48 h, the ability to dynamically upregulate glycolysis remained impaired. In patients, muscle capillarization was impaired, COX activity was reduced, and mitochondrial organization was disrupted. Moreover, transcription of Complex IV subunits COX5A and COX6A2 was, as in vibrated L6 cells, upregulated, suggesting a mismatch between transcript levels and protein expression. We conclude that snoring-induced vibrations are an unrecognized stressor that disrupts mitochondrial homeostasis in muscle by impairing RNA processing, protein synthesis, and mechanotransduction-driven mitochondrial remodeling, leading to transcript-protein uncoupling and likely muscle dysfunction. - Source: PubMed
Publication date: 2026/06/02
Stål PerEl-Habta RoineQian Yu-ChengZhu ShaochunWilliams ChloeMateus AndréGilthorpe Jonathan DShah Farhan - DEAD/H-box RNA helicases are critical regulators of host antiviral innate immunity. In this study, we utilized an RNA-binding protein knockout sub-library to identify DDX46, a member of the DEAD/H-box RNA helicase family, as an essential proviral host factor for RNA virus replication. While DDX46 has been shown to sequester demethylated innate immune transcripts in the nucleus and dampen interferon (IFN) production, the mechanisms underlying its regulation during viral infection remain unclear. Here, we report that RNA virus infection induces caspase-dependent cleavage of DDX46, triggering its translocation from the nucleus to the cytoplasm. This translocation unchains innate immune transcripts from nuclear retention, licensing their rapid translation and potentiating robust IFN responses. Our findings reveal a novel regulatory mechanism by which post-translational modification and subcellular relocalization of DDX46 fine-tune the host antiviral response, highlighting the functional versatility of RNA helicases in host-virus interactions.IMPORTANCEUnderstanding how host cells regulate innate immune responses to viral infection is essential for developing effective antiviral strategies. Our study uncovers a critical role for caspase-dependent cleavage and nuclear-cytoplasmic translocation of DDX46 in promoting antiviral innate immunity. These findings not only expand our knowledge of the dynamic regulation of DEAD/H-box RNA helicases during infection but also suggest that targeting the post-translational modification and localization of such helicases may offer new avenues for antiviral therapeutic development. - Source: PubMed
Publication date: 2026/03/19
Liu YanfengLiu ZhongyuanOu XiaoqingZhao FeiyangWang JingruiQu YangQiu XushengLiao YingTan LeiSong CuipingDing ChanSun Yingjie - O-linked-β-N-acetylglucosamine (O-GlcNAc) modification, also known as O-GlcNAcylation, is a dynamic and reversible protein modification. Aberrant O-GlcNAcylation are associated with the pathogenesis of cancers. DEAD-box helicase 46 (DDX46) is an ATP-dependent RNA helicase associated with cancer development; however, its role and regulation in hepatocellular carcinoma (HCC) remain unclear. In this study, we observed that the level of O-GlcNAcylation of DDX46 was significantly elevated in HCC mouse models and patients. In addition, direct OGT-DDX46 interaction facilitates O-GlcNAcylation at the Ser257 site. Mechanically, we discovered that O-GlcNAcylation enhances the stability of DDX46 by impeding ubiquitin-mediated degradation. Increased expression of DDX46 activates the PI3K/Akt signaling pathway, promoting the proliferation and invasion of HCC. Taken together, our study highlights the critical role of DDX46 O-GlcNAcylation in HCC progression, thus proposing targeted disruption of this cascade as a novel therapeutic strategy for HCC treatment. - Source: PubMed
Publication date: 2025/10/30
Wang QiujieLiu YuanyuanWang KaiHuang AilongTang NiPeng Pai - SF3B1 is the most frequently mutated splicing factor in cancer. Such mutations cause missplicing by promoting aberrant 3' splice site usage; however, how this occurs mechanistically remains controversial. To address this issue, we employed a computational screen of 600 splicing-related proteins to identify those whose reduced expression recapitulates mutant SF3B1-induced splicing dysregulation. Strikingly, our analysis reveals only two proteins whose knockdown or knockout reproduces this effect. Extending our previous findings, loss of the G-patch protein SUGP1 recapitulates almost all splicing defects induced by SF3B1 hotspot mutations. Unexpectedly, loss of the RNA helicase Aquarius (AQR) reproduces ∼40% of these defects. However, we find that AQR knockdown causes significant SUGP1 missplicing and reduced SUGP1 levels, suggesting that AQR loss reproduces mutant SF3B1 splicing defects only indirectly. This study advances our understanding of missplicing caused by oncogenic SF3B1 mutations and highlights the fundamental role of SUGP1 in this process. - Source: PubMed
Publication date: 2025/07/25
Xing PeiqiBak-Gordon PedroXie JindouZhang JianLiu ZhaoqiManley James L