SKIV2L2 antibody - N-terminal region (ARP36434_P050)
- Known as:
- SKIV2L2 (anti-) - N-terminal region (ARP36434_P050)
- Catalog number:
- arp36434_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SKIV2L2 antibody - N-terminal region (ARP36434_P050)
Related genes to: SKIV2L2 antibody - N-terminal region (ARP36434_P050)
- Gene:
- MTREX NIH gene
- Name:
- Mtr4 exosome RNA helicase
- Previous symbol:
- KIAA0052, SKIV2L2
- Synonyms:
- Mtr4, Dob1, fSAP118
- Chromosome:
- 5q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-02
- Date modifiied:
- 2017-11-24
Related products to: SKIV2L2 antibody - N-terminal region (ARP36434_P050)
Related articles to: SKIV2L2 antibody - N-terminal region (ARP36434_P050)
- BACKGROUND: Analyzing the content of immune cell-derived extracellular vesicles (EVs) may reveal biomarkers that elucidate the mechanisms through which infection negatively affects outcomes in patients with intracerebral hemorrhage (ICH). METHODS: A prospective observational study in patients with acute ICH classified by the occurrence of in-hospital infection within 7 days and outcomes at 6 months, good outcome defined as an improvement of > 10 points or > 50% in NIHSS score and a mRS score 0–2. Immune cell-derived EVs were obtained from blood samples at 7 days by immunoprecipitation with anti-CD3 (T cells), anti-CD20 (B cells) and anti-CD14 (monocytes) antibodies. The protein content of the EVs was analyzed by data independent acquisition mass spectrometry. Differential abundance between groups was defined as fold-change ≥ 2 or ≤ 0.5 and p ≤ 0.05. RESULTS: The study enrolled 44 patients: 17 (39%) infected, 14 (82%) with poor outcomes, and 27 (61%) with no infection, 12 (44%) with poor outcomes. There were 190 proteins with differential abundance in the EVs of infected patients, 6 relevant proteins associated with poor outcome and infection: in T cell-derived EVs PSME1 (involved in apoptosis), H2B1C and MTREX (involved in transcription regulation, DNA replication and DNA repair) were more abundant; in B cell-derived EVs, COHA1 (organization of extracellular matrix) was less abundant; and in monocyte-derived EVs, PCSK9 (cholesterol metabolism) and CMC1 (energy-related metabolic pathways) were less abundant. CONCLUSIONS: A cluster of proteins in immune system-derived EVs are involved in key biological pathways potentially linked to infection-related poor outcomes in patients with ICH. - Source: PubMed
Publication date: 2025/12/04
Laso-García FernandoAlonso-López ElisaPiniella DoloresDíez-Tejedor ExuperioGómez-de Frutos Mari CarmenCasado-Fernández LauraOtero-Ortega LauraLópez-Molina Mari PazGallego-Ruiz RebecaPozo-Novoa JavierCalzado-González ÁngelaDíaz-Gamero NereaRomán-San Martín AliciaBravo SusanaBarderas RodrigoDocando FélixFuentes BlancaJuárez-Martín BelénAlonso de Leciñana MaríaGutiérrez-Fernández María - NRDE2 is a highly conserved protein implicated in post-transcriptional gene silencing in and and has been shown to modulate splicing in mammals. To explore whether NRDE2 participates in additional processes in human cells, we performed tandem affinity purification followed by proteomic analysis of NRDE2 from nuclear extracts of HEK293T and HeLa cells. Our analysis confirmed the interaction of NRDE2 with its well-characterized partner, the MTR4 helicase (MTREX), as well as with multiple splicing factors. Notably, we also identified interactions with chromatin-associated proteins involved in transcription, including the Polymerase-Associated Factor 1 (PAF1) complex and elongating forms of RNA polymerase II (RNAPII). To further investigate NRDE2 function, we conducted RNA-seq following its transient depletion. Differential expression analysis revealed that loss of NRDE2 alters the expression of thousands of genes. Consistent with earlier reports, we observed splicing defects, particularly intron retention; however, our results indicate that the impact of NRDE2 on intron retention is more extensive than previously recognized. Moreover, intron retention was frequently associated with reduced mRNA expression. Together, these findings suggest that NRDE2 associates with both transcriptional and splicing machineries and plays a broader role in RNA processing than previously appreciated. - Source: PubMed
Publication date: 2025/10/08
Srbic MarinaBelhaouari ChaïmaaRaffel RaoulLemaire LaurineBarbier JeromeBossuyt JulieAkkawi CharbelContreras XavierKiernan Rosemary - The nucleolus is the largest membrane-less organelle within the nucleus and plays critical roles in regulating the cell cycle, senescence, and stress responses. The RNA exosome is a multiprotein ribonucleolytic complex involved in RNA processing and degradation in the cytoplasm, the nucleus, and the nucleolus. Previous studies have shown that the subcellular localization of the RNA exosome is crucial for its function. However, the mechanism that regulates its spatial distribution remains largely unexplored. In this study, we identified the nuclear RNA helicase MTR4 as a regulator of the RNA exosome localization through nucleolar quantitative proteomics technology. Immunostaining and fluorescence tagging confirmed that the depletion of MTR4 resulted in the translocation of the RNA exosome subunits from the nucleolus to the nucleoplasm. Notably, the translocation is specifically regulated by MTR4 and does not depend on other cofactors of the MTR4-containing Trf4/5-Air1/2-Mtr4 polyadenylation, poly(A) exosome-targeting, and nuclear exosome targeting complexes. The nucleolar accumulation of exosome subunits mutually depends on other exosome subunits. Additionally, actinomycin D treatment, which inhibits transcription, induced the RNA exosome to translocate from the nucleolus to the nucleoplasm, likely through the regulation of nucleolar MTR4 levels. These findings uncover a regulatory mechanism that modulates the localization of the RNA exosome within the nucleolus. - Source: PubMed
Publication date: 2025/07/10
Zhang YaqianJiang GuangzhenWang KeHong MinjieHuang XinyaChen XiangyangFeng XuezhuGuang Shouhong - HIV-1 latency is mainly characterized at transcriptional level, and little is known about post-transcriptional mechanisms and their contribution to reactivation. The viral protein Rev controls the nucleocytoplasmic export of unspliced and singly-spliced RNA that is central to proviral replication-competence and is therefore a prerequisite for efficient viral reactivation during the "shock-and-kill" cure therapy. Here we show that during infection and reactivation, unspliced HIV-1 RNA is a subject to complex and dynamic regulation by the Rev cofactor MATR3 and the MTR4 cofactor of the nuclear exosome. MATR3 and MTR4 coexist in the same ribonucleoprotein complex functioning to either maintain or degrade the RNA, respectively, with Rev orchestrating this regulatory switch. Moreover, we provide evidence of nuclear retention of unspliced HIV-1 RNA in ex vivo cultures from 22 ART-treated people with HIV, highlighting a reversible post-transcriptional block to viral RNA nucleocytoplasmic export that is relevant to the design of curative interventions. - Source: PubMed
Publication date: 2025/02/28
Dorman AgnieszkaBendoumou MaryamValaitienė AurelijaWadas JakubAli HaiderDutilleul AntoineMaiuri PaoloNestola LorenaBociaga-Jasik MonikaMchantaf GilbertNecsoi CocaDe Wit StéphaneAvettand-Fenoël VéroniqueMarcello AlessandroPyrc KrzysztofPasternak Alexander OVan Lint CarineKula-Pacurar Anna - - Source: PubMed
Yu LiliJiang LeiWu MengDou WenlongJi KaiyuanZhou JianlongKim JinchulXu Yang