Ask about this productRelated genes to: HNRPDL antibody
- Gene:
- HNRNPDL NIH gene
- Name:
- heterogeneous nuclear ribonucleoprotein D like
- Previous symbol:
- HNRPDL
- Synonyms:
- JKTBP, laAUF1
- Chromosome:
- 4q21.22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-25
- Date modifiied:
- 2015-11-09
Related products to: HNRPDL antibody
Related articles to: HNRPDL antibody
- Amyloids are traditionally associated with neurodegenerative and systemic diseases, yet it is now clear that they also perform essential physiological functions across kingdoms of life. Over the last decade, advances in cryogenic electron microscopy (cryo-EM) have enabled high-resolution structural characterization of functional amyloids, transforming our understanding of how the amyloid fold can be repurposed for biological activity. A landmark study in 2020 reported the cryo-EM structure of Orb2, a neuronal amyloid required for long-term memory persistence, establishing the first atomic view of a nuclear amyloid fibril. Subsequent structures of human RNA-binding proteins that form functional amyloids further expanded this paradigm. The structure of hnRNPDL-2 revealed how prion-like low-complexity domains can assemble into highly ordered, stable fibrils while keeping the necessary functionality for RNA metabolism. More recently, cryo-EM structures of the pigment-associated amyloid PMEL have provided insight into the molecular basis of melanosome biogenesis and pigmentation. In parallel, structural studies of bacterial functional amyloids, including the biofilm protein FapC, have uncovered architectures optimized for mechanical robustness and environmental resilience. Together, these pioneering studies reveal shared structural principles, alongside organism-specific adaptations that distinguish functional amyloids from their pathological counterparts. - Source: PubMed
Publication date: 2026/04/02
Ventura SalvadorBartolomé-Nafría AndreaGarcia-Pardo Javier - Autism spectrum disorder (ASD) is a pervasive neurodevelopmental condition characterized by social communication deficits, exhibiting a male bias in prevalence. Emerging evidence suggests that prenatal exposure to bisphenol A (BPA) may perturb neurodevelopmental trajectories relevant to ASD. While the cerebellum is increasingly recognized as a brain region implicated in ASD pathophysiology, the impact of gestational BPA exposure on its post-transcriptional alternative splicing machinery remains fundamentally undefined. - Source: PubMed
Publication date: 2026/06/22
Jantheang ThanawinKanlayaprasit SongphonSongsritaya KwanjiraPanjabud PawineeLertpeerapan PattanachatKasitipradit KasiditThongkorn SurangratJindatip DepichaHu Valerie WSaeliw ThanitSarachana Tewarit - This study aims to investigate the role of AU-rich element RNA-binding factor 1 (AUF1) in regulating inflammatory responses and senescence processes within auditory hair cells. - Source: PubMed
Publication date: 2026/05/26
Li LihuaXiao YunLiu XingruiHe JinyingWu WenjingCai DianChen Xubo - In the context of tumor diseases, aberrant splicing has become a potential source for targeted treatment. In this work, we discovered a 147-bp splicing anomaly in the downstream target gene BTC, which is regulated by the HNRNPDL gene in non-small cell lung cancer. The biological significance and therapeutic relevance of this splicing regulation remain unclear. - Source: PubMed
Publication date: 2026/03/11
Cao YujieLiu XiZhao RuijingLi YangGao HangyuYang YangYu JunLi Jianying - Long non-coding RNAs (lncRNAs) regulate antiviral immunity against influenza A viruses, yet their roles in natural reservoir hosts like ducks remain unclear. In ducks, Retinoic acid-inducible gene I (RIG-I) contributes to their resistance to infection. To identify duck lncRNAs involved in RIG-I-mediated antiviral responses, we analyzed transcriptomic data from highly pathogenic avian influenza (HPAI)-infected duck lung tissues and identified lnc455 co-expressed with IFNβ. In-silico predictions suggested lnc455 could interact with RIG-I and MAVS, two key signaling proteins in the Type I IFN pathway. Functional assays in chicken cells showed that lnc455 enhances IFNβ promoter activity when co-expressed with either RIG-I or MAVS, even in the absence of viral ligand. However, our data did not show direct binding between lnc455 and RIG-I or MAVS. Instead, lnc455 was associated with Type I IFN negative regulators, including Pur-α, Pur-β, YB-1, HNRNPDL, and HNRNPAB. Notably, overexpression of HNRNPAB reduced MAVS-induced IFNβ activity and MAVS protein abundance, effects that were significantly rescued by lnc455. These findings suggest that lnc455 enhances Type I IFN signaling indirectly by modulating MAVS-associated repression rather than through direct interaction with upstream sensors. Together, our results identify lnc455 as a duck-specific lncRNA that fine-tunes antiviral Type I IFN responses through indirect regulation of the RIG-I/MAVS signaling pathway. - Source: PubMed
Publication date: 2026/03/10
Legaspi Renald JamesMagor Katharine E