Ask about this productRelated genes to: LSM14A antibody
- Gene:
- LSM14A NIH gene
- Name:
- LSM14A mRNA processing body assembly factor
- Previous symbol:
- C19orf13, FAM61A
- Synonyms:
- DKFZP434D1335, RAP55A, RAP55
- Chromosome:
- 19q13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-11
- Date modifiied:
- 2019-01-25
Related products to: LSM14A antibody
Related articles to: LSM14A antibody
- Antiviral innate immune networks in human cells comprise core components that serve as central signaling hubs and several context-dependent modulators whose role may be virus- or tissue-specific. One such modulator is LSM14A, which potentiates innate immune response but is not essential. We recently showed that enteroviruses deploy their protease activity to cleave LSM14A, thereby disabling its antiviral function. In this study, we probe the molecular mechanism by which LSM14A contributes to innate immunity. We show that although LSM14A predominantly localizes to processing bodies (P-bodies; PBs), this localization is not essential for its innate immune function. Likewise, association with peroxisomes does not contribute to its immune activity. Instead, an unbiased systems-level interactomic analysis reveals a distinct cohort of LSM14A-associated proteins that assemble outside canonical PBs and peroxisomes following infection with Sendai virus, a robust inducer of innate immunity. Functional interrogation of these interactors demonstrate that several are essential for LSM14A-dependent amplification of antiviral signaling. Together, these findings uncover a functional axis of LSM14A that operates independently of its canonical subcellular localizations and is mediated through a specialized interaction network, improving our understanding of how this protein reinforces the antiviral innate immune system. - Source: PubMed
Publication date: 2026/05/12
Wacquiez AlanHboub HichamChen Da-YuanTavares Alexander HSu Chia-MingDe Paz JocelynSemaan MarcDing ZhenZaia JosephSethi Manveen KLyons Shawn MSaeed Mohsan - Blood-brain barrier (BBB) impermeability remains a major obstacle to the effective treatment of neurological disorders, particularly ischemic stroke. Here, we revealed that plant-derived extracellular vesicle-like nanoparticles (PEVs) offer a promising strategy to overcome this barrier. Using an optimized high-yield extraction protocol, we isolated PEVs from four medicinal plants: Panax ginseng, Panax notoginseng, Gastrodia elata, and Ligusticum chuanxiong. Among these, extracellular vesicles derived from Panax notoginseng (NotoEV, vesicle population) exhibited the strongest neuroprotective effects under hypoxic conditions in vitro and in vivo stroke models. Mechanistically, NotoEV delivered conserved plant microRNAs to recipient neurons, where they suppressed key stress granule nucleators GTPase-activating protein-binding protein 2 (G3bp2), Ubiquitin-associated protein 2 like (Ubap2l), and LSM14A mRNA processing body assembly factor (Lsm14a), activated mammalian target of rapamycin (mTOR) signaling, and promoted mitochondrial stabilization via the B-cell lymphoma 2 (Bcl-2)/ Translocase Of Outer Mitochondrial Membrane 20 (TOM20) axis. This cross-kingdom RNA delivery reprogrammed neuronal stress responses, reduced infarct volume, preserved neuronal morphology, and restored electrophysiological function. Collectively, our findings establish a scalable platform for plant-based nanotherapeutics and highlight the translational potential of NotoEV in treating ischemic stroke. - Source: PubMed
Publication date: 2026/02/13
Yu YuanyuanTan NaXu ZhifengTan ZhijianWang TaoLiu HuiminXu LeLu DanTang YameiMai Hongcheng - Pulmonary hypertension (PH) is a malignant progressive pulmonary vascular disease characterized by pulmonary vascular remodeling. Previous studies have shown that circRNAs mediated autophagy is associated with the occurrence and development of pulmonary hypertension, playing an important role in cell proliferation, apoptosis, and migration. Our aim is to investigate whether circular RNA is involved in autophagy of PH and its specific regulatory mechanisms. CircLSM14A is significantly down-regulated in hypoxic HPASMCs. The overexpression of circLSM14A inhibits hypoxia-induced HPASMCs autophagy in vivo and in vitro. Mechanically, by binding to its host protein LSM14A, circLSM14A enhances LSM14A ubiquitination, which in turn exerts an indirect inhibitory effect on LSM14A-regulated YBX1 SUMOylation, leading to the transcriptional regulation of downstream autophagy genes. In addition, Silencer interacts with the LSM14A promoter region to recruit ZNF281, thereby mediating transcriptional repression of circLSM14A. In summary, this paper reveals a novel circRNA that inhibits HPASMC autophagy via the host protein LSM14A, which has the potential to be a new target for PH therapy. - Source: PubMed
Publication date: 2026/02/10
Gao DanniSong ShashaGao YupeiZhu XinlongYuan HaoGuan XiaoyuMa CuiFu QiangQin WenZhang LixinWang ShanshanChen BoZhu Daling - The innate immune system relies on pattern recognition receptors (PRRs) to detect viral pathogens and initiate antiviral responses. LSM14A, a conserved RNA-binding protein involved in mRNA metabolism, has recently emerged as a cytosolic nucleic acid sensor in vertebrates. However, its role in teleost immunity remains unclear. In this study, two LSM14A paralogs were identified in grass carp (Ctenopharyngodon idella), designated CiLSM14Aa and CiLSM14Ab, and their functions during infection with grass carp reovirus genotype II (GCRV-II) were investigated. Both CiLSM14Aa and CiLSM14Ab were significantly upregulated following GCRV-II infection or poly(I:C) stimulation. Overexpression of CiLSM14Aa or CiLSM14Ab inhibited GCRV-II replication and enhanced the expression of type I interferon and interferon-stimulated genes (ISGs). Further analysis revealed that CiLSM14Aa and CiLSM14Ab can form homodimers and heterodimers. Notably, only CiLSM14Aa demonstrated direct binding to double-stranded RNA (dsRNA), suggesting a specific role as a cytosolic dsRNA sensor. These results demonstrate the essential antiviral roles of CiLSM14A paralogs and reveal their contributions to the initiation of innate immune defenses against GCRV-II infection. - Source: PubMed
Publication date: 2026/01/27
Jiang HuiZhang ChuLi PengfeiZhang Yong-AnQin Xiangmou - In response to stress, cells undergo gene expression reprogramming to cope with external stimuli. Cells utilize a conserved stress response mechanism called global downregulation of translation, leading to the storage of translationally repressed mRNAs in RNA granules. During oxidative stress induced by H2O2, genes responsible for combating oxidative stress, such as catalases, are strongly induced. However, the post-transcriptional regulatory events affecting these genes during H2O2 stress are not well-explored. Scd6, an RGG-motif-containing protein in yeast, acts as a translational repressor through its interaction with eIF4G1. This study identifies the role of Scd6 in oxidative stress response by regulating cytoplasmic catalase T1 (CTT1). We observe that peroxide stress induces the assembly of Scd6 puncta, which do not colocalize with P-bodies or stress granules. Scd6 overexpression increased sensitivity, while deletion enhanced tolerance to H2O2 treatment. Increased ROS accumulation and decreased Ctt1 protein levels were observed upon Scd6 overexpression due to translation repression of CTT1 mRNA. CTT1 mRNA interacts with Scd6. smFISH analysis and RNA immunoprecipitation studies reveal that localization of Scd6 to puncta upon peroxide stress reduces its interaction with CTT1 mRNA, allowing derepression. The role of Scd6 in peroxide stress response is conserved since the human homolog LSm14A also localizes to puncta upon H2O2 stress, and its overexpression reduces survival in response to peroxide stress. Overall, this study identifies a unique example of translation regulation whereby stress-induced localization of the translation repressor protein to puncta leads to derepression of the target mRNA. - Source: PubMed
Publication date: 2026/01/09
Tiwari SwetaTogra ChitraSj SudharshanRajyaguru Purusharth I