Ask about this productRelated genes to: DHX38 antibody
- Gene:
- DHX38 NIH gene
- Name:
- DEAH-box helicase 38
- Previous symbol:
- DDX38
- Synonyms:
- PRP16, KIAA0224, hPrp16, PRPF16
- Chromosome:
- 16q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-11
- Date modifiied:
- 2016-10-05
Related products to: DHX38 antibody
Related articles to: DHX38 antibody
- 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 - Exome sequencing solved 26% of nephronophthisis cases, identifying nephropathy and extrarenal disease genes beyond classic ciliopathy panels. Exome sequencing uncovered GN and tubular nephropathy genes misdiagnosed as ciliopathy-associated nephropathy, underscoring diagnostic overlap in kidney diseases. Patients with nonciliary genetic variants may present with ciliopathy-like extrarenal symptoms, showing phenocopies in kidney ciliopathy diagnostics. - Source: PubMed
Publication date: 2025/12/04
Petzold FriederikeJeanpierre CécileChen XiaoyiMorinière VincentBenmerah AlexandreDorval GuillaumeSaei HassanHeidet LaurenceAntignac CorinneSaunier Sophie - Accurate splicing, which involves the controlled removal of non-coding sequences (introns) from precursor messenger RNAs (pre-mRNAs), is essential for producing correct mature mRNAs that encode functional proteins. Within pre-mRNAs, latent splice sites (LSSs) resemble proper splice sites but are usually not used because their activation can introduce in-frame STOP codons. The nuclear suppression of splicing (SOS) mechanism prevents the use of LSSs. Although the SOS mechanism is not fully understood, recent studies have identified initiator-tRNA and the NCL protein as key components. To discover additional regulators, we performed a genetic screen targeting RNA-binding proteins (RBPs) with an siRNA library and a luminescence reporter for latent splice site activation. This identified five RBPs - ALYREF (THOC4), PPIE, DDX41, DHX38, and HNRNPA2B1 - whose knockdown significantly increased LSS usage in the reporter. RNA-Seq analysis after knocking down each of these RBPs confirmed these results, showing widespread LSS activation in hundreds of mRNAs. Among these, we focused on ALYREF, a conserved protein involved in mRNA export and splicing. Using fPAR-CLIP, we found that U5 snRNA is ALYREF's main binding partner. Overexpressing ALYREF deletion mutants activated latent splicing, and affinity purification confirmed its interaction with U5 snRNA. These mutants exhibited different binding properties, highlighting the importance of specific structural elements within ALYREF in SOS regulation. Our findings reveal that nuclear RBPs play a key role in suppressing LSS activation and suggest that ALYREF has a novel role in maintaining splicing accuracy within the spliceosome, advancing our understanding of the SOS mechanism. - Source: PubMed
Publication date: 2025/07/23
Arafat MaramGotea ValerUmar Mubarak IMuharram AyaKamhi EyalAgami ReuvenSperling JosephHafner MarkusElnitski LauraSperling Ruth - N6-methyladenosine (m A) modification of mRNA is a critical post-transcriptional regulatory mechanism that modulates mRNA metabolism and neuronal function. The m A reader YTHDF1 has been shown to enhance the translational efficiency of m A-modified mRNAs in the brain and is essential for learning and memory. However, its role in the mature retina remains unclear. Herein, we report a novel role of in the maintenance of retinal function using a genetic knockout model. Loss of resulted in impaired scotopic electroretinogram (ERG) responses and progressive retinal degeneration. Detailed analyses of rod photoreceptors confirmed substantial degenerative changes in the absence of ciliary defects. Single-cell RNA sequencing revealed comprehensive molecular alterations across all retinal cell types in -deficient retinas. Integrative analysis of methylated RNA immunoprecipitation (MeRIP) sequencing and RIP sequencing identified and , two inheritable retinal degeneration disease-associated gene homologs, as direct targets of YTHDF1 in the retina. Specifically, YTHDF1 recognized and bound m A-modified and mRNA at the coding sequence (CDS), enhancing their translational efficiency without altering mRNA levels. Collectively, these findings highlight the essential role of YTHDF1 in preserving visual function and reveal a novel regulatory mechanism of m A reader proteins in retinal degeneration, identifying potential therapeutic targets for severe retinopathies. - Source: PubMed
Zhu Xian-JunJiang Xiao-YanLiu Wen-JingFan Yu-DiLiu GuoYao ShunSun Kuan-XiangChen Jun-YaoLei BoYang Ye-Ming - : Alternative splicing is essential for the physiological and pathological development of the inner ear. Disruptions in this process can result in both syndromic and non-syndromic forms of hearing loss. DHX38, a DEAH box RNA helicase, is integral to pre-mRNA splicing regulation and plays critical roles in development, cell differentiation, and stem cell maintenance. However, its specific role in inner ear development remains undefined. Here, we utilized a knockout zebrafish model to monitor the ear morphology and elucidate a crucial role for DHX38 in the development of the zebrafish inner ear. : Bright-field morphological analysis and in situ hybridization were performed to observe ear morphology changes. Immunofluorescence and semi-quantitative RT-PCR were employed to test apoptotic cells and abnormal splicing. : The mutant zebrafish showed significant inner ear impairments, including decrescent otocysts, absent semicircular canal protrusion, and smaller otoliths. These structural abnormalities were accompanied by substantial DNA damage and p53-dependent apoptosis within the inner ear cells. Alternative splicing analysis showed that genes related to DNA damage repair and inner ear morphogenesis are abnormal in knockout mutants. In summary, we suggest that promotes cell survival during the inner ear development of zebrafish by ensuring the correct splicing of genes related to DNA damage repair. - Source: PubMed
Publication date: 2024/12/26
Ren MengmengChen XiangDai LiyanTu JiayiHu HualeiSun XiaohanLuo JiongLi PeiFu YiyangZhu YuejieSun WeiqiangTang ZhaohuiLiu MugenRen XiangLu Qunwei