Ask about this productRelated genes to: DHX16 antibody
- Gene:
- DHX16 NIH gene
- Name:
- DEAH-box helicase 16
- Previous symbol:
- DDX16
- Synonyms:
- DBP2, Prp2, PRPF2
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-04
- Date modifiied:
- 2016-10-05
Related products to: DHX16 antibody
Related articles to: DHX16 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 - Retinitis pigmentosa and sensorineural deafness are two distinct clinical entities that can be caused by a variety of genetic mutations. The gene, which encodes a protein involved in RNA processing, has been implicated in several genetic disorders. Here, we report a unique case of gene mutation presenting with both retinitis pigmentosa and sensorineural deafness. - Source: PubMed
Publication date: 2026/01/05
Wang LeiGao JiyongSun MengFan LiWang ShuhuaLi XueGu ShuangyuHan Bingjuan - Pathogenic variants in DEAH-box helicase 16 (DHX16) that are critical regulators of mRNA metabolism have been linked to neuromuscular oculoauditory syndrome (NMOAS), a rare disorder characterized by sensorineural hearing loss, neuromuscular deficits, and retinal abnormalities. This report covers a rare case of a 6-month-old girl with congenital SNHL, global hypotonia, and distinctive bilateral retinal dystrophy. Eye exam revealed severe macular atrophy with peripheral pigmentary changes. Spectral-domain optical coherence tomography confirmed outer retinal thinning and disruption of the photoreceptor integrity. Whole trio genome sequencing identified a heterozygous variant in DHX16, c.1360C>T (p.Arg454Trp), previously described in only one patient, and classified as likely pathogenic. This case expands the understanding of DHX16-associated NMOAS and the importance of comprehensive ophthalmological assessment and genetic analysis in infants with multisystem involvement. - Source: PubMed
Publication date: 2025/10/07
Yun Justin SYamamoto Marcus HMarin Alejandro ISargiotto CarlaSchweitzer Daniela NTsui Irena - Although recent investigations have identified a novel regulatory cascade involving female determiner (fmd), female determiner 2 (fmd2), and doublesex (dsx) in Hemiptera species, the evolutionary conservation and molecular mechanisms governing the fmd/fmd2-dsx pathway remain poorly characterized. The small brown planthopper, Laodelphax striatellus (Hemiptera: Delphacidae), represents an ideal model system for elucidating the evolutionary dynamics of sex determination pathways, as its underlying mechanism remains undefined. Here, we demonstrate that the fmd2 homolog (Lsfmd2) in L. striatellus is functionally involved in sex determination through a specific splicing isoform, LsFMD2, the protein of which contains a specific carboxyl-terminal sequence - GTGGGYGGGGKQRGGGRGQRHTPY. Functional characterization in 293T cells revealed that LsFMD2 interacts with LsFMD-F to regulate female-specific splicing of Lsdsx. Importantly, we identified DHX16, an ATP-dependent RNA helicase and pre-messenger RNA splicing factor, as a novel binding partner of LsFMD2. RNA interference-mediated depletion of DHX16 resulted in the ectopic expression of male-specific Lsdsx isoforms in female individuals and induced significant ovipositor malformations. Intriguingly, while LsFMD2 exhibited simultaneous binding capacity with both LsFMD-F and LsDHX16, no direct interaction was observed between LsDHX16 and LsFMD-F, indicating that LsFMD2 serves as a molecular scaffold in the fmd/fmd2/DHX16-dsx regulatory cascade. These findings provide robust evidence for the evolutionary conservation of the fmd/fmd2-dsx regulatory cascade across Hemiptera species. Moreover, the newly identified component DHX16 significantly enhances our mechanistic understanding of this non-canonical sex determination pathway. - Source: PubMed
Publication date: 2025/05/06
Chen YouyuanMao ZepingGao YangweiWang HaiqiangYing JinjunWang LinWang XinghuaXiao ShanChen JianghuaLi JunminZhang ChuanxiZhuo Jichong - DHX16, a member of the DexD/H-box RNA helicase family, facilitates ATP-dependent unwinding of RNA secondary structures. Pathogenic variants cause poor functioning of the spliceosome complex leading to intron retention in gene transcripts. Clinically, it is associated with neuromuscular oculoauditory syndrome (MIM #618733). To date, there are nine published cases. We report a tenth case: a 3-year-old female, initially presented at 7 months of age, with mild developmental delay, ocular anomalies, dysmorphia, and increased infections. An inherited retinal disorder panel identified nondiagnostic variants of uncertain significance. Trio exome sequencing revealed a de novo Likely Pathogenic DHX16 variant, c.692G>C; p.R231P. Published cases of DHX16-related disorders report developmental delay/intellectual disability, seizures, myopathy, retinal anomalies, myopia, nystagmus, and hearing loss. No published variants to date are located upstream of the start of the helicase domain, and little is known about upstream domains. In silico analysis demonstrates evidence of pathogenicity, while Missense3D modeling demonstrates no structural damage to the protein. These findings are consistent with current literature, suggesting a mechanism of pathogenicity that is difficult to assess via modeling. This case illustrates a DHX16 variant in an unknown domain displaying a mild phenotype. - Source: PubMed
Publication date: 2025/05/06
Clay SloaneLeon AlejandroWall Luke AZambrano Regina M