Ask about this productRelated genes to: AP1G1 antibody
- Gene:
- AP1G1 NIH gene
- Name:
- adaptor related protein complex 1 subunit gamma 1
- Previous symbol:
- CLAPG1, ADTG
- Synonyms:
- -
- Chromosome:
- 16q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2000-09-01
- Date modifiied:
- 2018-04-23
Related products to: AP1G1 antibody
Related articles to: AP1G1 antibody
- Lung cancer remains the leading cause of cancer mortality. The AP-1 adaptor complex, including AP1AR, AP1S1, AP1S2, AP1S3, AP1M1, AP1M2, AP1B1, and AP1G1, functions as a conserved hub of vesicular trafficking, selecting cargo and coordinating clathrin-mediated transport. By shaping receptor recycling, membrane composition, and signal duration, AP-1 influences core cancer phenotypes such as proliferation, migration, and therapy response. However, the family-level role of AP-1 adaptors in lung cancer is incompletely defined. We systematically profiled all eight AP-1 adaptor genes using multi-omics datasets, survival resources, pharmacogenomic panels, Human Protein Atlas data, pathway enrichment, and single-cell RNA sequencing with cell-cell communication modeling. was consistently upregulated in lung adenocarcinoma and independently associated with poorer overall survival. It was linked to cell-cycle progression, DNA replication checkpoints, hypoxia, and epithelial-to-mesenchymal transition (EMT). At single cell resolution, also regulate malignant epithelial and fibroblast cell types. Pseudotime analyses revealed progressive activation along proliferative and EMT axes, and CellChat modeling indicated enhanced stromal and epithelial signaling. and showed complementary roles, associated with oncogenic/inflammatory signaling and immune-metabolic programs, respectively. These findings identify as a clinically relevant biomarker and highlight AP-1 adaptor biology as an underexplored contributor to lung adenocarcinoma progression and therapeutic stratification. - Source: PubMed
Publication date: 2026/01/01
Solomon Dahlak DanielYeh I-JengLiu Hsin-LiangSu Che-YuLee Yung-KuoKo Ching-ChungLin Hui-RuKumar SachinXuan Do Thi MinhPalekkode NeethuFathima AymanLin Hung-YunWang Chih-YangYen Meng-Chi - Autism spectrum disorder (ASD) is a neurodevelopmental condition marked by difficulties in social interactions, communication impairments, repetitive behaviors, and restricted interests. A genetic basis for ASD is now well-established. With the availability of high-throughput microarray and sequencing platforms, major advances have been made in our understanding of genetic risk factors. This study assessed the patient records of 62 children diagnosed with ASD or at risk for ASD. Cytogenetics, molecular karyotyping, and whole-exome sequencing (WES) were conducted for these cases. Three likely pathogenic variants were detected in the genes KMT2C, FOXP2, and MAN1B1, each at a rate of 1.6% of total cases. Additionally, variants of uncertain significance (VUS) were found in 13 genes previously associated with ASD. The frequencies of these VUS in total cases were as follows: DLG3-1.6%, MECP2-1.6%, SETD5-1.6%, GRIN1-1.6%, ASXL3-3%, KMT2D - 5%, AP1G1-3%, SPTBN1-3%, TRIP12-1.6%, HCN1-3%, ZNF292-1.6%, and ACSL4-1.6%. We found gene variants in 35% of cases, a rate consistent with previous reports, emphasizing the importance of comprehensive genetic analysis in diagnosing ASD with unclear etiology. This study offers valuable insights into the genetic landscape of ASD within a small cohort and highlights the need for ongoing monitoring and genetic counseling in conditions that present with ASD-like symptoms. - Source: PubMed
Publication date: 2025/12/20
Eser MetinHekimoglu GulamKutlubay Busra - Adaptor Protein-1 (AP-1) is a heterotetrameric essential for intracellular vesicular trafficking and polarized localization of somato-dendritic proteins in neurons. Variants in the gene, encoding the gamma-1 subunit of adaptor-related protein complex 1 (AP1γ1), have recently been associated with Usmani-Riazuddin syndrome (USRISD, MIM#619467), a very rare human genetic disorder characterized by intellectual disability (ID), speech and neurodevelopmental delays. Here we report a novel variant (c.196G>A; p.Gly66Arg) identified by exome sequencing analysis in a young girl showing overlapping clinical features with USRIS, such as motor and speech delay, intellectual disability and abnormal aggressive behavior. In silico analysis of the missense de novo variant suggested an alteration in AP1G1 protein folding. Patient's fibroblasts have been studied with immunofluorescence techniques to analyze the intracellular distribution of AP-1. Zebrafish are widely regarded as an excellent vertebrate model for studying human disease pathogenesis, given their transparent embryonic development, ease of breeding, high genetic similarity to humans, and straightforward genetic manipulation. Leveraging these advantages, we investigated the phenotype, locomotor behavior, and CNS development in zebrafish embryos following the microinjection of human wild-type and mutated mRNAs at the one-cell stage. Knockout (KO) of the gene in zebrafish led to death at the gastrula stage. Lethality in the KO fish model was significantly rescued by injection of the human wild-type mRNA, but not by transcripts encoded by the Gly66Arg missense allele. The phenotype was also not rescued when zebrafish embryos were co-injected with both human wild-type and mutated mRNAs, supporting the dominant-negative effect of the new variant. In this study, we defined the effects of a new variant in cellular and animal models of Usmani-Riazzudin syndrome for future therapeutic approaches. - Source: PubMed
Publication date: 2025/10/30
Imperatore ValentinaMirarchi AlessandraAgolini EmanueleAstolfi AndreaBarreca Maria LetiziaNovelli AntonioVinciarelli ElisaFerretti SaraZizioli DanielaBorsani GiuseppeArcuri CataldoProntera Paolo - Traditional antiviral strategies primarily rely on vaccines and virus protein-targeting drugs, which adopt a virus-targeting approach. However, the rapid mutation of viruses often leads to vaccine failure and drug resistance, highlighting the limitations of these conventional methods. Consequently, the development of novel broad-spectrum, host-targeting antiviral strategies has become a major research focus. Itaconate, an endogenous immunomodulatory metabolite, inhibits viral replication via post-translational modifications; however, its mechanism in suppressing viral endocytosis remains unclear. This study demonstrates that itaconate inhibits viral endocytosis by covalently modifying the Cys128 site of the adaptor-related protein complex 1 gamma 1 subunit (AP1G1), thereby providing a new target for host-directed antiviral drug development. It was found that itaconate binds to AP1G1 at Cys128, impairing its interaction with clathrin, which inhibits clathrin-mediated viral particle uptake and reduces cellular susceptibility to infection (i.e., the likelihood of cells being infected by viruses and undergoing infection). Furthermore, the natural product Licochalcone B was identified as targeting the same site as itaconate. In both BEAS-2B cell models and mouse infection models, Licochalcone B reduced pulmonary viral loads by over 95%. This study is the first to propose and validate the feasibility of inhibiting broad-spectrum viral infection by targeting AP1G1, elucidating a novel molecular mechanism of itaconate-mediated regulation, offering a new target for broad-spectrum antiviral drug development, and identifying Licochalcone B as a promising broad-spectrum antiviral agent. - Source: PubMed
Publication date: 2025/11/10
Deng XinqiChen HengHuang ZhixingHe RonggeRao QinlingXu LuniXu ZijianZhao NaixuanPeng YeqingLi MuxuanLiu XiMa TaoCui XiaolanWang Chunguo - Modulating cell endocytosis activity to reduce host susceptibility to virus represents a promising strategy for antiviral drug development. In this study, we reveal that lactate transporter SLC16A3 is a critical host factor for reducing diverse virus invasion. By performing metabolomics, proteomics, and thermal proteome profiling experiments, AP1G1, a pivotal protein involved in cellular endocytosis, was indiscriminately screened as a chaperone of SLC16A3. SLC16A3 decides the membrane enrichment of AP1G1 by protein interaction, thereby influencing host susceptibility to diverse viruses. This conclusion was further validated in SLC16A3 knocked-down cells, which indicated a broad-spectrum target for anti-virus drug development to recede virus entry by blocking the interaction between AP1G1 and SLC16A3. This conclusion has been validated with a patent medicine Shufengjiedu (SFJD). SFJD exhibits strong effect in decreasing the susceptibility of host cells to viral infections. Molecularly, SFJD administration results in disrupting the interaction between SLC16A3 and AP1G1 and reduced membrane localization of AP1G1. Consequently, it achieves a receded endocytosis activity of host cells on viral particles. This provides evidence for the practicability of the SLC16A3-AP1G1 strategy. Taken together, the regulation on the SLC16A3-AP1G1 interaction represents a broad-spectrum and practicable antiviral strategy. This study offers insights into a novel approach for inhibiting viral infections through the alteration of host susceptibility and advances the idea for antiviral drug development.IMPORTANCEWe have discovered that a broad-spectrum antiviral strategy, highlighting the lactate transporter SLC16A3 as a critical determinant of host cell susceptibility to viruses. SLC16A3 was found to interact with AP1G1, which is a pivotal protein involved in cellular endocytosis. Disrupting the interaction between AP1G1 and SLC16A3 leads to reduced membrane localization of AP1G1, thereby reducing the host cell endocytosis of viral particles. Importantly, we found that the patent medicine Shufengjiedu (SFJD can significantly reduce the susceptibility of host cells to viral infection through this mechanism, providing evidence for the practicability of SLC16A3-AP1G1 strategy. Taken together, the modulation on the SLC16A3-AP1G1 interaction represents a broad-spectrum and practicable antiviral mechanism. This study offers novel insights into strategies for inhibiting viral infections through the alteration of host susceptibility and advances the idea for antiviral drug development. - Source: PubMed
Publication date: 2025/09/08
Deng XinqiHe RonggeZhang JingshengRao QinglingChen HengHuang ZhixingHu ZiYiCao ShanWang ZiyuGuo ShanshanWang ChunguoCui Xiaolan