Ask about this productRelated genes to: RARRES3 antibody
- Gene:
- PLAAT4 NIH gene
- Name:
- phospholipase A and acyltransferase 4
- Previous symbol:
- RARRES3
- Synonyms:
- TIG3, HRASLS4, PLAAT-4, RIG1
- Chromosome:
- 11q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-03
- Date modifiied:
- 2019-02-14
Related products to: RARRES3 antibody
Related articles to: RARRES3 antibody
- Not available. - Source: PubMed
Publication date: 2026/06/11
Guiraud VincentBravetti ClotildeGuihot AmélieDenis Jérôme AlexandreLegrand RonanCharlotte FrédéricLe Garff-Tavernier MagaliParizot ChristopheFouquet BaptisteHouot RochDulery RemyMarcelin Anne-GenevieveCalvez VincentBarete StéphaneTodesco EveChoquet Sylvain - Eukaryotic genomes contain numerous transposable elements (TEs), whose dysregulation threatens genome stability and may contribute to cancer. Pancreatic adenocarcinoma (PAAD) is among the deadliest cancers, marked by abundant stroma that obscures tumor-specific molecular signals, complicating bulk-tissue analyses. Here, using 71 patient-derived PAAD organoids, we show that TE activities may potentially promote tumorigenesis and provide a source of novel immunotherapeutic targets. We identify 16 new TE-derived transcripts fused with 15 known oncogenes, exhibiting potential oncogenic function and prognostic value. Notably, -, present in 29% of tumors, encodes a protein variant transcriptionally regulated by binding to the promoter. - isoform 2 is associated with increased cholesterol ester accumulation and lipid droplet formation mediated through coexpression, potentially fostering tumor progression. On the immunogenic front, HLA-I immunopeptidomics of AsPC-1 cells and DAC13 organoids identify over 11,000 peptides respectively. Althought mutation-derived neoantigens are rare, several peptides are originated from TE-chimeric transcripts, including four predicted by TEprof2. The peptide FLIQHLPLV, detected in 27% of organoids, exhibits robust immunogenicity, validated by T2 binding, mass spectrometry and ELISPOT assays with HLA-genotyped PBMCs. Together, these findings suggest that TE activities may contribute to PAAD progression and diversify its immunopeptidome, providing new opportunities for molecular subtyping and potential immunotherapeutic intervention. - Source: PubMed
Publication date: 2026/02/03
Shi MeilongTeng ChuanqiZhang ShanHe XiaoboXu LingyunHan FengxianWen RongqiYu GanjunLiu JingwenFeng YangWu YanfengRen YanJin GangLi Jing - Cervical cancer progression is intricately linked to dysregulated cell death pathways, particularly PANoptosis, a coordinated form of programmed cell death. However, prognostic biomarkers and immunological implications of PANoptosis-related genes (PRGs) in cervical cancer remain underexplored. - Source: PubMed
Publication date: 2025/11/22
Tong YuehongDeng WeiXu LiliLi YaoZhang Keke - B-cell lymphoma 6 (BCL6) is increasingly recognized as a driver of cancer progression; however, the precise molecular mechanisms by which BCL6 facilitates high-grade serous ovarian cancer (HGSOC) progression remain incompletely understood. - Source: PubMed
Publication date: 2025/07/24
Wan AnZhao Wei-DongChen GangPeng ChengTao Jin-Hui - Non-small cell lung cancer (NSCLC) is a highly prevalent and aggressive cancer with a high incidence. While cellular retinoic acid binding protein 2 (CRABP2) has been implicated in tumor progression, metastasis and drug resistanceacross multiple cancer types, its functional role and molecular mechanisms of CRABP2 in NSCLC progression remain largely unexplored. In this study, we demonstrated that CRABP2 expression was significantly elevated in NSCLC tissues compared to adjacent normal tissues, and high levels of CRABP2 correlated with reduced overall survival. Functionally, knockdown of CRABP2 inhibited NSCLC cell proliferation, migration, and invasion, and lipid droplet accumulation , while CRABP2 targeting inhibited tumor growth, lipid droplet content and metastasis in xenograft model. Mechanistically, CRABP2 was identified to bind to Phospholipase A/acyltransferase 4 (PLAAT4) and decreases its protein stability. Notably, inhibition of PLAAT4 reverses the shCRABP2-induced suppression of malignant phenotypes and lipid droplet formation. our findings reveal a novel CRABP2/PLAAT4-mediated lipid metabolic axis drives NSCLC progression and metastasis. These findings suggest that targeting CRAPB may offer a novel approach to therapeutic intervention for NSCLC. - Source: PubMed
Publication date: 2025/06/23
Xia JiePeng BiWang JianhuaLi FangLong Guoxian