Ask about this productRelated genes to: RBM42 antibody
- Gene:
- RBM42 NIH gene
- Name:
- RNA binding motif protein 42
- Previous symbol:
- -
- Synonyms:
- MGC10433
- Chromosome:
- 19q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2007-05-01
- Date modifiied:
- 2019-03-19
Related products to: RBM42 antibody
Related articles to: RBM42 antibody
- Dendrite regeneration is critical for restoring neuronal connectivity after injury, yet the underlying molecular mechanisms remain poorly understood. Using as a model and through a forward genetic screen, we identified the conserved insulin degrading enzyme and the RNA-binding protein as key regulators of dendrite regeneration, where functions upstream of . We further show that , one of the core components of the phagocytosis pathway, acting down stream of , while other components of this pathway don't play significant roles in dendrite regeneration. In addition, we demonstrate that upon injury IDR-1 can promote RBM-42 nuclear export following injury, enabling its dendritic localization. RBM-42, in turn, promotes the translation of and facilitates microtubule assembly. In conclusion, our findings define a novel conserved signaling cascade coupling injury-induced nuclear export of RNA binding proteins to local regulation and dendrite regeneration, providing new mechanistic insight into neuronal repair. - Source: PubMed
Publication date: 2025/11/18
Qu ZhongweiYan Dong - is a key oncogenic driver frequently overexpressed in non-small cell lung carcinoma (NSCLC) and other cancers, where its protein levels often exceed what would be expected from mRNA levels alone, suggesting post-transcriptional regulation. Strategies to inhibit function by targeting mRNA translation hold potential for therapeutics utility in Myc-dependent cancers. We developed TranslationLight, a high-content imaging platform which detects mRNA translation in human cells. Using this system, we conducted a high-throughput screen of ~100,000 compounds to identify small molecules that selectively modulate translation. Candidate compounds were evaluated by immunofluorescence, ribosome profiling, RNA sequencing, cellular thermal shift assays (CETSA), and subcellular localization studies of mRNA and RNA-binding proteins. We identified a lead compound, CMP76, that potently reduces Myc protein without substantially decreasing its mRNA abundance. Mechanistic investigations showed that the compound induces relocalization of mRNA into stress granules, accompanied by translational silencing. CETSA identified hnRNPK as a primary protein target, and compound treatment triggered its cytoplasmic relocalization together with formation of hnRNPK-containing granules colocalizing with mRNA. Analysis across cancer cell lines revealed that sensitivity to CMP76 was significantly associated with RBM42 dependency. This work establishes a novel therapeutic strategy to inhibit translation mediated by hnRNPK, offering a translationally targeted approach to cancer therapy. - Source: PubMed
Publication date: 2025/08/22
Sheinberger YoniWassermann RinaKhier JasmineKassa EphremVaturi LinoySlonim NaamaTverskoi ArtemMandaby AviadDemishtein AlikKlepfish MordehayShapira-Lots InbalAlroy Iris - Oncogenic protein dosage is tightly regulated to enable cancer formation but how this is regulated by translational control remains unknown. The Myc oncogene is a paradigm of an exquisitely regulated oncogene and a driver of pancreatic ductal adenocarcinoma (PDAC). Here we use a CRISPR interference screen in PDAC cells to identify activators of selective MYC translation. The top hit, the RNA-binding protein RBM42, is highly expressed in PDAC and predicts poor survival. We show that RBM42 binds and selectively regulates the translation of MYC and a precise suite of pro-oncogenic transcripts, including JUN and EGFR. Mechanistically, we find that RBM42 binds and remodels the MYC 5' untranslated region structure, facilitating the formation of the translation pre-initiation complex. Importantly, RBM42 is necessary for PDAC tumorigenesis in a Myc-dependent manner in vivo. This work transforms the understanding of the translational code in cancer and illuminates therapeutic openings to target the expression of oncogenes. - Source: PubMed
Publication date: 2025/02/04
Kovalski Joanna RSarioglu GoksuSubramanyam VishvakHernandez GraceRademaker GillesOses-Prieto Juan ASlota MaceyMohan NimmyYiakis KayleeLiu IsabelleWen Kwun WahKim Grace EMiglani SohitBurlingame Alma LGoodarzi HaniPerera Rushika MRuggero Davide - Oncogenic protein dosage is tightly regulated to enable cancer cells to adapt and survive. Whether this is regulated at the level of translational control and the key factors in and remain unknown. The Myc oncogene is a central paradigm of an exquisitely regulated oncogene and a major driver of pancreatic ductal adenocarcinoma (PDAC). Using a functional genome-wide CRISPRi screen in PDAC cells, we identified activators of selective translation through its 5' untranslated region (5'UTR) and validated four RNA binding proteins (RBPs), including epitranscriptome modifiers. Among these RBPs, our top hit was RBM42, which is highly expressed in PDAC and predicts poor survival. Combining polysome sequencing and CLIP-seq analyses, we find that RBM42 binds and selectively regulates the translation of and a precise, yet vital suite of pro-oncogenic transcripts, including and . Mechanistically, employing IP-mass spectrometry analysis, we find that RMB42 is a novel ribosome-associated protein (RAP). Using DMS-Seq and mutagenesis analysis, we show that RBM42 directly binds and remodels the 5'UTR RNA structure, facilitating the formation of the translation pre-initiation complex. Importantly, RBM42 is necessary for human PDAC cell growth and fitness and PDAC tumorigenesis in xenograft mouse models in a Myc-dependent manner . In PDAC patient samples, RBM42 expression is correlated with Myc protein levels and transcriptional activity. This work transforms our understanding of the translational code in cancer and offers a new therapeutic opening to target the expression of oncogenes. - Source: PubMed
Publication date: 2024/10/11
Kovalski Joanna RSarioglu GoksuSubramanyam VishvakHernandez GraceRademaker GillesOses-Prieto Juan ASlota MaceyMohan NimmyYiakis KayleeLiu IsabelleWen Kwun WahKim Grace EMiglani SohitBurlingame Alma LGoodarzi HaniPerera Rushika MRuggero Davide - p53-mediated cell cycle arrest during DNA damage is dependent on the induction of p21 protein, encoded by the CDKN1A gene. p21 inhibits cyclin-dependent kinases required for cell cycle progression to guarantee accurate repair of DNA lesions. Hence, fine-tuning of p21 levels is crucial to preserve genomic stability. Currently, the multilayered regulation of p21 levels during DNA damage is not fully understood. Herein, we identify the human RNA binding motif protein 42 (RBM42) as a regulator of p21 levels during DNA damage. Genome-wide transcriptome and interactome analysis reveals that RBM42 alters the expression of p53-regulated genes during DNA damage. Specifically, we demonstrate that RBM42 facilitates CDKN1A splicing by counteracting the splicing inhibitory effect of RBM4 protein. Unexpectedly, we also show that RBM42, underpins translation of various splicing targets, including CDKN1A. Concordantly, transcriptome-wide mapping of RBM42-RNA interactions using eCLIP further substantiates the dual function of RBM42 in regulating splicing and translation of its target genes, including CDKN1A. Collectively, our data show that RBM42 couples splicing and translation machineries to fine-tune gene expression during DNA damage response. - Source: PubMed
Publication date: 2023/11/22
Ben-Oz Bella MMachour Feras ENicola MarianArgoetti AmirPolyak GaliaHanna RawadKleifeld OdedMandel-Gutfreund YaelAyoub Nabieh