Ask about this productRelated genes to: LSM2 antibody
- Gene:
- LSM2 NIH gene
- Name:
- LSM2 homolog, U6 small nuclear RNA and mRNA degradation associated
- Previous symbol:
- C6orf28
- Synonyms:
- G7b, YBL026W
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-05
- Date modifiied:
- 2016-10-05
Related products to: LSM2 antibody
Related articles to: LSM2 antibody
- Spermatogenesis requires precise spatial and temporal regulation of RNA splicing, orchestrated by both the major (U1, U2, and U4/U6/U5) and minor (U11, U12, and U4atac/U6atac/U5) spliceosomal small nuclear ribonucleoproteins (snRNPs), yet their function during germ cell development remain poorly defined. Here, we elucidate the essential function of LSM7, a component of the LSM2-8 complex, in snRNP biogenesis and the process of spermatogenesis. Our results demonstrate that LSM7 governs the stability of U6 small nuclear RNA (snRNA) within Cajal bodies and directly interacts with scaRNA2, scaRNA13, and scaRNA17 to modulate 2'-O-methylation and pseudouridylation modifications of U2 and U12 snRNAs. Loss of LSM7 results in defective nuclear localization and reduced stability of U2, U5, and U6 snRNAs, destabilization of their corresponding snRNP complexes, and aberrant splicing events, notably affecting mutually exclusive exons and exon skipping. These splicing defects lead to translational dysregulation, ultimately impairing the differentiation of spermatogonial stem cells into spermatogonia. Our findings identify LSM7 as a pivotal regulator linking scaRNA-guided snRNA modifications, spliceosomal fidelity, and the determination of spermatogonial stem cell fate, offering important mechanistic insights into the post-transcriptional regulation of male germ cell development. - Source: PubMed
Publication date: 2026/05/21
Qi HangChen Si-YuMi Jin-QiaoFan Wei-HongHu Feng-JieLi Qiao-DanChang HuanLi Zhi-YiLin Xiao-DieWang Xiao-XiaFan Pei-YinJiang YuLi You-JiangWu Jing-GenXiao Ying-PingFan Heng-YuCai JieXu JianDai Xing-Xing - Telomerase biogenesis is a multistep process requiring the coordinated action of several accessory factors. In the fission yeast Schizosaccharomyces pombe, the telomerase RNA TER1 undergoes spliceosome-mediated 3'-end processing, followed by association with the Pof8/Bmc1/Thc1 complex, which facilitates binding of the Lsm2-8 complex. Lsm2-8 protects TER1 from nucleolytic degradation and promotes recruitment of the catalytic subunit Trt1. Here, we identify Pop6, Pop7, and Pop100, three subunits of the RNase P/MRP complex, as components of the active telomerase holoenzyme. These proteins associate with a stem-loop-stem structure near the TER1 pseudoknot that resembles the P3 domain found in RNase P/MRP RNAs. A single-nucleotide change within this P3-like loop disrupts Pop protein binding, resulting in reduced telomerase activity and severe telomere shortening. This mutation also impairs the assembly of key telomerase subunits and alters the folding of the template-pseudoknot region of TER1. Our findings reveal a critical role for Pop6, Pop7, and Pop100 in chaperoning TER1 into a conformation that promotes functional telomerase assembly and underscore the remarkable evolutionary plasticity of telomerase biogenesis. - Source: PubMed
Publication date: 2026/04/28
Pan LiliPatterson ValentineMöckel Martin MHelston Rachel MWellinger Raymund JZappulla David CBaumann Peter - Post-transcriptional maturation of the U6 snRNA 3'-end, important for spliceosome assembly, is catalyzed by sequential actions of TUT1 and USB1. It is believed that the TUT1-catalyzed oligo(U) tail at the U6 snRNA 3'-end serves merely as a substrate for USB1 to generate a final 2',3'-cyclic phosphate group to mature the U6 snRNA. However, biallelic inactivation of TUT1 or USB1 is linked to distinct human developmental disorders, suggesting that they have different physiological functions. Here, using genetically engineered mouse models, we show that Tut1 is required to maintain stem cell pools during embryogenesis, whereas unexpectedly Usb1 is dispensable for this. Loss of Tut1 weakens the interaction of the U6 snRNA with the Lsm2-8 protein complex, causes defective RNA splicing, and triggers massive DNA damage and subsequent cell death. Splicing defects and cell death can be mitigated by recombinant U6 snRNA containing an oligo(U) tail. We propose that the TUT1-catalyzed oligo(U) tail is essential for splicing and cell proliferation. Further modification of this oligo(U) tail by USB1 is ubiquitous but only functionally required in specific cell types. - Source: PubMed
Publication date: 2026/04/09
Fang YinQiu TongLuo HongWang YanYang ChaoWang MinDai QianZheng WenyueYin RutieXiao XueLi Qintong - The Solute carrier family 25 member 3 (SLC25A3), a mitochondrial solute carrier protein, has been implicated in tumor progression. Nonetheless, the connection between SLC25A3 and hepatocellular carcinoma (HCC) remains ambiguous. - Source: PubMed
Publication date: 2026/01/24
Bie BeibeiLiu LibingWang FurongMeng XianingWu MengdiSun Jin - Fusarium graminearum, the causal agent of Fusarium head blight (FHB), poses a major threat to global food security by contaminating cereals with the mycotoxin deoxynivalenol (DON). Although transcriptional and protein-level regulation of its stress response and virulence has been extensively studied, the functional significance of mRNA processing in these critical processes remains largely unexplored. Here, we identify Lsm8, a highly conserved core subunit of the nuclear Lsm2-8 complex, as a pivotal regulator linking RNA splicing fidelity to fungal growth, stress adaptation, and virulence. Deletion of LSM8 disrupted Lsm2-8 assembly and nuclear localization, resulting in widespread intron retention in genes essential for stress signaling (HOG1, ATF1), development (GPA1, STE12), and trichothecene biosynthesis. Consequently, osmoadaptation was impaired, sexual reproduction was abolished, and both DON production and virulence were drastically reduced. We further demonstrate that intron-retained transcripts are predominantly degraded by the RNA exosome, revealing a conserved Lsm8-exosome module that maintains splicing fidelity and RNA surveillance. Given the deep evolutionary conservation of Lsm8 across eukaryotes, these findings uncover a fundamental post-transcriptional regulatory layer governing fungal stress response, virulence, and mycotoxin biosynthesis, and highlight RNA-processing factors as universal determinants of virulence and promising antifungal targets across eukaryotic pathogens. - Source: PubMed
Publication date: 2026/02/10
Ren YiyiCheng HaolanHan XingminGuo MeilingXu ChenghuiYan JiayueGe ZhiweiMa ZhonghuaChen Yun