Ask about this productRelated genes to: DHX8 Blocking Peptide
- Gene:
- DHX8 NIH gene
- Name:
- DEAH-box helicase 8
- Previous symbol:
- DDX8
- Synonyms:
- HRH1, PRP22, PRPF22, Dhr2
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1995-12-20
- Date modifiied:
- 2017-05-26
Related products to: DHX8 Blocking Peptide
Related articles to: DHX8 Blocking Peptide
- DHX8 encodes a DEAH-box RNA helicase, an ATP-dependent enzyme that plays essential roles in RNA metabolism, including pre-mRNA splicing, transcription, and mRNA decay. Although DHX8 dysfunction has been linked with developmental abnormalities and disease pathogenesis in multiple model organisms, its biological functions in Lepidoptera, particularly in the silkworm , remain unknown. To investigate the developmental role of . DHX8 (BmDHX8), we generated knockout mutants using CRISPR-Cas9 genome editing. Genome sequencing confirmed frameshift mutations in the BmDHX8 locus. BmDHX8 mutants exhibited severe developmental defects such as dramatically reduced body size and premature lethality of silkworm larvae. Molecular characterization suggested systemic dysregulation, as evidenced by decreased triglyceride accumulation, impaired mTOR signaling activity, and increased aberrant splicing events. Therefore, these results indicate that loss of BmDHX8 is associated with aberrant splicing and alterations in lipid homeostasis and mTOR signaling pathways, potentially contributing to developmental defects. Taken together, our study offers an initial functional knockout analysis of BmDHX8 in regulating larval development in silkworms. - Source: PubMed
Publication date: 2026/02/25
Ding LingXu CexinZhang YunxiaoWang YuanboHou YongShen GuanwangLin PingXia QingyouZhao PingLi Zhiqing - Transcription factor heat shock factor 1 (HSF1) orchestrates the cellular stress response, promoting malignant transformation, unchecked proliferation, and stress-resilient survival of tumour cells. We set out to discover potentially druggable regulators of HSF1 activation and identified DEAH-box RNA helicase 8 (DHX8). We investigated the role of DHX8 in regulating HSF1 within the broader context of DHX8 function in cancer cells. DHX8 silencing induces intron retention in transcripts, reducing HSF1 protein. Importantly, DHX8 loss significantly alters RNA processing of an HSF1-regulated cancer-associated gene signature linked to poor clinical outcomes, as well as additional oncogenic and stress-response pathways. DHX8 binds between the pre-messenger RNA (mRNA) lariat branch point and the 3' splice site, consistent with the predominance of intron-retained transcripts following DHX8 loss. We show that both the ATPase and RNA-binding activities of DHX8 are essential for its role in splicing, including processing of mRNA. We also find that DHX8 silencing triggers apoptosis more effectively in human cancer cells than in non-tumorigenic cells. Our findings identify DHX8 as a critical regulator of stress-adaptive gene expression, highlighting its promise as a therapeutic target not only to disrupt HSF1-dependent transcriptional programs but also having broader effects in cancer cells under oncogenic stress. - Source: PubMed
Publication date: 2026/03/12
Tall Jennifer RTe Poele RobertVasile AlexandraRamagiri PradeepCampbell JamesDavies Caitlin RPowers Marissa VRoe TobySankaran DeivendranWang HannahMitsopoulos KonstantinosAl-Lazikani Bissanvan Montfort Rob L Mde Billy EmmanuelWorkman PaulClarke Paul A - Pre-mRNA splicing is orchestrated by the spliceosome through coordinated RNA and protein rearrangements driven by ATP-dependent RNA helicases. DEAH-box helicases serve as principal motors, controlling catalytic activation, exon ligation, and complex disassembly. Early mechanistic understanding was limited by low-resolution cryo-electron microscopy (cryo-EM) structures, leaving RNA substrate interactions largely inferred from biochemical and genetic studies. Recent high-resolution cryo-EM structures (2021-present) have captured all five spliceosomal DEAH-box helicases-DHX16/Prp2, DHX38/Prp16, DHX8/Prp22, DHX15/Prp43, and DHX35-bound to their RNA targets within distinct spliceosomal states. These structures reveal precise recruitment, substrate recognition, and stage-specific actions. In this review, I integrate these insights into a unified framework, highlighting structural, biochemical, and evolutionary perspectives to guide future investigations of helicase regulation and their role in maintaining the fidelity of eukaryotic RNA splicing. - Source: PubMed
Chen Zhe - : Using fish collagen supplements in daily nutrition may positively influence health and healthy aging. However, their systemic, molecular-level effects on humans are not well characterized. Therefore, given the scarcity of proteomic data, this study aimed to assess the serum proteomic changes during the fish collagen supplementation in healthy women. : This was a crossover interventional study. Thirty healthy women received either 5 mL of fish gel collagen (from silver carp: ) supplementation with 200 mL of pure water for 40 days or 200 mL of pure water for 40 days only. The washout between the fish collagen and pure water supplementation was 40 days. The nutritional status and dietary intake were assessed. Proteome analyses were conducted using a MALDI-TOF mass spectrometer in a positive linear mode in the / 1000-10,000 range. : The diet of the women in this study was not well-balanced. Supplementation did not affect nutritional status. Only water content significantly increased. During the fish collagen supplementation, the following discriminative proteins were identified: Filamin-A, Filamin-B, actin, Vimentin, Tropomyosin beta chain, 40S ribosomal protein S8, ATP-dependent RNA helicase DHX8, and FERM domain-containing protein 4A. : Changes in serum proteins may reflect broader cytoskeletal remodeling and cellular adaptation resulting from collagen intake. - Source: PubMed
Publication date: 2025/09/24
Stelmach-Mardas MartaMatuszewska-Mach ElizaKustra KrzysztofPietkiewicz DagmaraMatysiak JanHojan-Jezierska DorotaMardas MarcinKubisz Leszek - RNautophagy is an intracellular degradation pathway in which RNA is directly taken up by lysosomes. The cytoplasmic regions of the lysosomal membrane proteins, LAMP2C and SIDT2, can interact with consecutive guanine sequences in RNA, mediating the uptake of RNA during RNautophagy. RNautophagy has also been implicated in the clearance of expanded CAG-repeat mRNA and RNA foci associated with polyQ disease. However, the mechanisms of RNA uptake during RNautophagy remain unclear. Here, we screened for proteins that bind consecutive guanine sequences and identified RNA helicase DHX8 as a binding partner. DHX8 interacts with SIDT2 and is partially localized to the cytoplasmic side of the lysosomal membrane. We found that DHX8 regulates intracellular RNA degradation via SIDT2-dependent RNautophagy but not via macroautophagy. RNA binding, but not ATPase activity, of DHX8 is likely to be important for regulating RNA degradation. DHX8 also contributes to the clearance of pathogenic CAG repeat mRNA and RNA foci, and the levels of both soluble protein and insoluble high-molecular-weight aggregates of expanded polyQ tracts. Our findings provide insights into the mechanisms underlying the regulation of intracellular RNA degradation, autophagic pathways, and possibly the pathogenesis of repeat RNA-related disorders. - Source: PubMed
Sakai RyoheiTakeda EigoKabuta ChihanaContu Viorica RalucaFujiwara YuukiFujikake NobuhiroHashimoto TadafumiOhsumi YoshinoriKabuta Tomohiro