Ask about this productRelated genes to: RBM7 Blocking Peptide
- Gene:
- RBM7 NIH gene
- Name:
- RNA binding motif protein 7
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11q23.1-q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-01
- Date modifiied:
- 2015-06-04
Related products to: RBM7 Blocking Peptide
Related articles to: RBM7 Blocking Peptide
- CCR4-NOT complex is involved in transcription, translation, and mRNA degradation. As of yet, it is unknown if CCR4-NOT has additional functions beyond those. It is possible to predict unknown functions of genes by using co-expressed network analysis. Here we show that all CCR4-NOT subunits highly co-express with modulators of small nuclear noncoding RNA biogenesis, predicting that CCR4-NOT regulates the maturation of small nuclear noncoding RNA. In agreement with this, knockdown of CNOT1 decreased the expression levels of small nuclear non-coding RNAs independent of the canonical function of CCR4-NOT complex. However, the reduced expression was rescued by the co-suppression of RBM7, mediating exosomal degradation of misprocessed small RNA. These results suggest that CNOT1 contributes to small nuclear non-coding RNA maturation. - Source: PubMed
Publication date: 2025/12/23
Umehara ChisatoSakurai ReikaSako HiroakiYamamoto Tadashi - Temozolomide (TMZ) resistance is a major cause of treatment failure in glioblastoma (GBM). This study investigates the role and mechanism of the RNA-binding protein RNA-binding motif protein 7 (RBM7) and F-box and leucine-rich repeat protein 16 (FBXL16) in TMZ resistance in GBM, focusing on mitochondrial dysfunction and ferroptosis. TMZ-resistant GBM cell lines (TR/U87) were established through gradient induction. Cell viability and proliferation were assessed using the Cell Counting Kit-8 assay and colony formation assays. Western blot analysis and immunohistochemistry were performed to measure FBXL16, activating transcription factor 4, and peroxisome proliferator-activated receptor gamma coactivator 1-alpha protein expression. Transwell assays evaluated TR/U87 cell migration and invasion. Co-immunoprecipitation and RNA immunoprecipitation assays verified the interaction between RBM7 and FBXL16. An actinomycin D assay analyzed FBXL16 mRNA stability. Flow cytometry was used to detect reactive oxygen species, iron levels, and apoptosis. A nude mouse xenograft model was used to validate in vivo effects. RBM7 was highly expressed in TMZ-resistant cells. Knockdown of RBM7 suppressed TR/U87 cell proliferation and migration, induced mitochondrial structural damage, and triggered ferroptosis. Mechanistically, RBM7 interacted with FBXL16 and reduced its mRNA stability. FBXL16 knockdown reversed RBM7 deficiency-induced ferroptosis and chemosensitivity. In vivo experiments confirmed that RBM7 knockdown combined with TMZ significantly inhibited tumor growth. RBM7 promotes TMZ resistance by suppressing mitochondrial dysfunction and ferroptosis through destabilization of FBXL16. Targeting the RBM7-FBXL16 axis may represent a novel strategy to overcome GBM chemoresistance. - Source: PubMed
Publication date: 2025/12/12
Liu NanCui YeTingLi JuanLi SuMeiTu YanYangHuo JunLiZhang TongCunZhen HaiNing - To evaluate cognitive impairment in patients with chronic heart failure (CHF) and its impact on treatment adherence. - Source: PubMed
Publication date: 2025/07/31
Aksenova Y OPetrukhina A AOsmolovskaya Y FZhirov I VBeniashvili A GMorozova M ARupchev G EGalich A ATolstukhina O NTereshchenko S N - In mammalian cells, primary miRNAs are cleaved at their hairpin structures by the Microprocessor complex, whose core is composed of DROSHA and DGCR8. Here, we show that 5' flanking regions, resulting from Microprocessor cleavage, are targeted by the RNA exosome in mouse embryonic stem cells (mESCs). This is facilitated by a physical link between DGCR8 and the nuclear exosome targeting (NEXT) component ZCCHC8. Surprisingly, however, both biochemical and mutagenesis studies demonstrate that a variant NEXT complex, containing the RNA helicase MTR4 but devoid of the RNA-binding protein RBM7, is the active entity. This Microprocessor-NEXT variant also targets stem-loop-containing RNAs expressed from other genomic regions, such as enhancers. By contrast, Microprocessor does not contribute to the turnover of less structured NEXT substrates. Our results therefore demonstrate that MTR4-ZCCHC8 can link to either RBM7 or DGCR8/DROSHA to target different RNA substrates depending on their structural context. - Source: PubMed
Imamura KatsutoshiGarland WilliamSchmid ManfredJakobsen LisSato KengoRouvière Jérôme OJakobsen Kristoffer PorsBurlacu ElenaLopez Marta LoureiroLykke-Andersen SørenAndersen Jens SJensen Torben Heick - The PP2A-B55 phosphatase regulates a plethora of signaling pathways throughout eukaryotes. How PP2A-B55 selects its substrates presents a severe knowledge gap. By integrating AlphaFold modeling with comprehensive high-resolution mutational scanning, we show that α helices in substrates bind B55 through an evolutionary conserved mechanism. Despite a large diversity in sequence and composition, these α helices share key amino acid determinants that engage discrete hydrophobic and electrostatic patches. Using deep learning protein design, we generate a specific and potent competitive peptide inhibitor of PP2A-B55 substrate interactions. With this inhibitor, we uncover that PP2A-B55 regulates the nuclear exosome targeting (NEXT) complex by binding to an α-helical recruitment module in the RNA binding protein 7 (RBM7), a component of the NEXT complex. Collectively, our findings provide a framework for the understanding and interrogation of PP2A-B55 function in health and disease. - Source: PubMed
Publication date: 2024/10/02
Kruse ThomasGarvanska Dimitriya HVarga Julia KGarland WilliamMcEwan Brennan CHein Jamin BWeisser Melanie BiancaBenavides-Puy IkerChan Camilla BachmanSotelo-Parrilla PaulaMendez Blanca LopezJeyaprakash A ArockiaSchueler-Furman OraJensen Torben HeickKettenbach Arminja NNilsson Jakob