Ask about this productRelated genes to: WDR37 antibody
- Gene:
- WDR37 NIH gene
- Name:
- WD repeat domain 37
- Previous symbol:
- -
- Synonyms:
- KIAA0982
- Chromosome:
- 10p15.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-06
- Date modifiied:
- 2014-11-19
Related products to: WDR37 antibody
Related articles to: WDR37 antibody
- - Source: PubMed
Publication date: 2026/08/03
Cerdá Checa SusanaVizcaíno Díaz CarolinaFernández Martínez Cristian - BACKGROUND: Silicosis is a severe occupational pulmonary fibrosis disease caused by silica dust inhalation, characterized by persistent inflammation and progressive fibrosis. While transcriptomic studies have identified numerous genes dysregulated, molecular mechanisms extend beyond mere changes in gene expression levels. Recent evidence suggests that post-transcriptional regulatory mechanisms, particularly alternative splicing (AS), may play crucial roles in fibrotic processes. However, AS dynamics and functional significance in silicosis remain largely unexplored. METHOD: To investigate AS in silicosis pathogenesis, we analyzed RNA sequencing (RNA-Seq) data from a mouse model, delineating the dynamic landscape of gene expression and AS events across disease stages. AS events were classified into two categories: those correlated with and independent of gene expression changes. We integrated single-cell RNA sequencing (scRNA-seq) data to precisely map the cell type-specific expression patterns of these events. Through this analysis, we identified critical AS events, whose dynamic regulation and functional relevance during silicosis progression were validated using in vivo and in vitro models. RESULTS: A total of 26,232 high-confidence AS events were identified, with Skipping Exon (SE) being the predominant type (75.6%, 19,832/26,232). These splicing events were derived from 7,524 parental genes, with 72% (5,422) harboring at least two events, indicating widespread splicing complexity. 1,363 (5.2%) high-confidence events were significantly regulated across disease stages, with 88 Differentially Expressed Alternative Splicing (DEAS) events exhibiting a substantial splicing shift (absolute delta Percent Spliced In (PSI) greater than 0.2). Strikingly, only 11.4% (10/88) of these DEAS events showed concordant gene-level changes, while a substantial proportion (88.6%, 78/88) occurred despite stable gene level expression. Parental genes were enriched in silicosis-related pathways, including smooth muscle cell migration, actin bundle assembly and the small GTPase-mediated signal transduction. Integrated scRNA-seq helped map expression to specific cell types and prioritize validation targets. The dynamic regulation of three top targets, including Clec4e- Retained Intron (RI), Wdr37- Alternative First Exon (AFE), and Tns3-AFE, was validated in mouse models. In vitro functional experiments showed that Clec4e isoforms (RI and non-RI) possess distinct functional properties; dysregulation of Clec4e-RI may relieve inflammatory inhibition. These results suggest a potential regulatory role of AS reprogramming in silicosis pathogenesis and indicate Clec4e splicing events as a possible target for inflammation regulation. CONCLUSION: This study presents a landscape of AS in silicosis, demonstrating that AS constitutes a critical layer of pathological regulation distinct from transcriptional alterations. We identified and validated that the Clec4e-RI splicing isoform may play a key role in the silicosis pathogenesis by modulating macrophage-related inflammatory responses. - Source: PubMed
Publication date: 2026/04/23
Luo JinqinOu SiyangWang XinmiaoWang Yin-YingYang LuoJiang JingwenXu JueZhu GuanghuiChen Sujun - Phosphofurin acidic cluster sorting protein 1 (Pacs1) is a multidomain adaptor proposed to bind transmembrane cargo proteins to facilitate their intracellular trafficking. Pacs1 also forms a complex with WD-repeat protein 37 (Wdr37), which is essential for lymphocyte homeostasis. Despite numerous proposed binding partners, a validated structure for Pacs1-containing protein complexes is lacking. Here, we present the cryo-electron microscopy structure of the Pacs1-Wdr37 complex. Pacs1 binds Wdr37 through a conserved interface within its furin-binding region (FBR), the domain previously linked to cargo recognition. This interaction stabilizes Wdr37 and is critical for the expression of both proteins. A gain-of-function mutation in (R203W) causes a highly penetrant neurodevelopmental syndrome. This pathogenic mutation lies on a solvent-exposed surface of the FBR and does not disrupt complex formation. Instead, Pacs1-R203W remains dependent on Wdr37 for stability and its levels can be reduced through targeted Wdr37 proteolytic degradation. Structural homology of the FBR to synaptotagmin C2 domains reveals a previously unrecognized ability of Pacs1 to bind negatively charged phospholipids through a unique positively charged cleft. Together these findings define the structural basis for Pacs1-Wdr37 complex assembly and stability, present potential strategies for Pacs1-mediated neurodevelopmental disease, and suggest novel Pacs1 functions in membrane association. - Source: PubMed
Publication date: 2025/11/05
Xiao LeGrzemska MagdalenaPi XiongChen LumingTurner MichaelPeddada NageshCalvache SamanthaJia JessicaBeutler BruceWu HaoNair-Gill Evan - Despite significant advances in gene discovery, the molecular basis of many rare genetic disorders remains poorly understood. The concept of disease modules, clusters of functionally related genes whose disruption leads to overlapping phenotypes, offers a valuable framework for interpreting these conditions. However, identifying such relationships remains particularly challenging in ultra-rare syndromes due to the limited number of documented cases. We hypothesized that AI-based facial phenotyping could aid in identifying shared molecular mechanisms by detecting phenotypic convergence among clinically related syndromes. To test this, we used Schuurs-Hoeijmakers syndrome (SHMS; OMIM #615009), caused by a recurrent de novo variant in , as a model to explore potential phenotypic and functional associations with -related disorder (DEE66; OMIM #618067) and -related disorder (NOCGUS; OMIM #618652). Facial photographs of individuals with SHMS were analyzed using the DeepGestalt and GestaltMatcher algorithms. In addition to consistently recognizing SHMS as a distinct clinical entity, the algorithms frequently matched DEE66 and NOCGUS, suggesting a shared facial gestalt. Binary comparisons further confirmed overlapping craniofacial features among the three disorders. These findings were supported by literature review, indicating clinical overlapping and potential functional associations. Overall, our results confirm the presence of consistent facial similarities among -, -, and -related syndromes and highlight the utility of AI-driven facial phenotyping as a complementary tool for uncovering clinically relevant relationships in ultra-rare genetic disorders. - Source: PubMed
Publication date: 2025/08/18
Del Rincón JuliaGil-Salvador MartaLucia-Campos CristinaAcero LauraTrujillano LauraArnedo MaríaPamplona PilarAyerza-Casas AriadnaPuisac BeatrizRamos Feliciano JPié JuanLatorre-Pellicer Ana - Growth traits are one of the most important economic traits in pigs, including body weight and average daily gain. However, the available genetic markers for these traits are limited, especially concerning Chinese indigenous pigs and their hybrid breeds. - Source: PubMed
Publication date: 2025/07/11
Sun KailingHong YuanZhang WenyuDong JiangpengWen ZuohaoHu ZhengyuTan XuhuiLi HaoZhao AyongHuang MinHuang Tao