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
- G-patch proteins are emerging as key regulatory cofactors of DEAH-box RNA helicases involved in pre-mRNA splicing, yet the functions of many family members remain poorly understood. Here, we characterize the conserved G-patch domain-containing protein Cwf28 from Schizosaccharomyces pombe, an essential factor with a previously unclear molecular function, and define its role within the spliceosome. Tandem affinity purification coupled with mass spectrometry revealed that Cwf28 predominantly associates with components of the Prp19 complex (NTC) and factors involved in the catalytic activation and progression of the spliceosome, placing it within catalytically active spliceosomal assemblies. Gene ontology analysis showed enrichment of the Cwf28 interactome in factors involved in spliceosome assembly, activation, and catalytic remodeling. Notably, the DEAH-box RNA helicase Cdc28, the ortholog of human DHX16 and Saccharomyces cerevisiae Prp2, was identified as the most abundant interactor. Further analysis demonstrated that Cwf28 interacts with Cdc28 via its conserved G-patch domain, and domain mapping confirmed that this interaction is G-patch domain dependent. Together, these findings identify Cwf28 as a component of catalytically active spliceosomes and suggest a potential role for Cwf28 in modulating the activity of the RNA helicase Cdc28, providing insight into conserved mechanisms underlying RNA helicase regulation during splicing. - Source: PubMed
Publication date: 2026/09/03
Karika Laura OliviaCipakova IngridKretova MiroslavaSelicky TomasCmikova NataliaNemcekova DanielaKohutova LenkaBarath PeterCipak Lubos - Neuromuscular oculoauditory syndrome (NMOAS; OMIM# 618733) is a rare neurodevelopmental disorder caused by heterozygous variants in DHX16, a gene in the DExD/H-box RNA helicase family. Despite increasing reports of DHX16-related NMOAS, the functional impact of specific variants on RNA splicing remains poorly understood. In this study, whole-exome sequencing identified a de novo DHX16 variant (c.1360C>G, p.Arg454Gly) in a 2-year-old boy with NMOAS. In vitro assays revealed aberrant intron retention in HSPH1 and FOS transcripts in cells expressing the mutant DHX16-1360G, suggesting impaired splicing efficiency. Longitudinal clinical follow-up uncovered progressive multisystem involvement, including delayed gonadal development and autism spectrum disorder phenotypes not previously linked to DHX16. These findings expand the genotypic and phenotypic spectrum of NMOAS, confirm the pathogenic role of this variant in splicing dysregulation, and emphasize the need for long-term monitoring of emerging comorbidities in affected patients. - Source: PubMed
Publication date: 2026/08/06
Shen YueZhou YunyuLu ChaoCao ZongfuYu YufeiCheng TingtingGao HuafangLuo MinnaMa XuSui Ruifang - 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