PRMT4 Assay Kit_Luminescent
- Known as:
- PRMT4 Assay Kit_Luminescent
- Catalog number:
- 52041
- Product Quantity:
- 96 reactions
- Category:
- Peptides
- Supplier:
- Biotech support group
- Gene target:
- PRMT4 Assay Kit_Luminescent
Related genes to: PRMT4 Assay Kit_Luminescent
- Gene:
- CARM1 NIH gene
- Name:
- coactivator associated arginine methyltransferase 1
- Previous symbol:
- -
- Synonyms:
- PRMT4
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-14
- Date modifiied:
- 2016-11-11
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- A key driver of Glioblastoma (GBM) heterogeneity and therapy resistance is the capacity of glioma stem-like cells (GSCs) to hijack developmental signaling programs. However, it remains unclear how GSCs regulate these adapted developmental signaling pathways and how these pathways might be therapeutically exploited. The arginine methyltransferase, CARM1, has been shown to play critical roles in maintaining stem cell pluripotency, preventing differentiation, and recently was discovered to be upregulated in Glioblastoma. To date, there is little to no understanding of the role that CARM1 plays in regulating developmental processes in Glioblastoma. To address this gap in knowledge, we applied a multi-omics approach to characterize developmental processes that are specifically regulated by CARM1 in GSCs. We found that loss of CARM1 results in dysregulation of several developmental markers: ARX, GFAP, NGFR, PDGFRA and results in both a proteomic and transcriptomic shift towards the radial glia cell lineage. Moreover, CARM1 depleted cells reprogram their signaling to develop an increased survival dependency on NGFR/NTRK signaling and are hypersensitive to the FDA approved brain penetrant NTRK inhibitor-Entrectinib. Mechanistically, we find that NFIA is a CARM1 substrate and can repress NGFR signaling just as CARM1 does, and thus the CARM1/NFIA relationship is likely a key regulator of NGFR/NTRK signaling in GSCs. Altogether, we demonstrate that CARM1 regulates the cell lineage of GSCs at the transcriptomic and proteomic level, and naturally represses NGFR/NTRK signaling-likely through CARM1 dependent methylation of NFIA. Further, CARM1 depletion leads GSCs to develop a survival dependency on NGFR/NTRK signaling and creates a therapeutic vulnerability to NTRK inhibition. - Source: PubMed
Publication date: 2025/04/17
Young Dejauwne LAguilan JenniferCutler RonaldStransky StephanieDeAngelo Joseph DRoth Jacob SMalachowska BeataVercellino JustinBell Brett IShechter DavidTofilon Philip JPhillips Richard EGuha ChandanSidoli Simone - The structure-specific endonuclease, XPF-ERCC1, plays a central role in DNA damage repair. This nuclease is known to be important for nucleotide excision repair, interstrand crosslink repair, and DNA double-strand repair. We found that the arginine methyltransferase, CARM1/PRMT4, is essential for XPF stabilization and maintenance of intracellular protein levels. Loss of CARM1 results in a decrease in XPF protein levels and a concomitant decrease in ERCC1 protein. A similar destabilization of XPF protein was observed in cells expressing a mutant in which XPF arginine 568 was replaced by lysine. Loss of CARM1 impaired XPF-ERCC1 accumulation at the site of damage and delayed removal of cyclobutane pyrimidine dimers by UV. As a result, CARM1-deficient cells showed increased UV sensitivity. Our results provide insight into the importance of CARM1 not only in the mechanism of XPF-ERCC1 complex stabilization but also in the maintenance of genome stability. - Source: PubMed
Niida HiroyukiIto MasahikoIijima KentaMotegi AkiraOgihara RinAkiyama HironobuUchida ChiharuSakai SatoshiOhhata TatsuyaHatano AtsushiHirose MichikoOgura AtsuoMatsumoto MasakiMcDonald Neil QKitagawa Masatoshi - Sunitinib resistance remains a major obstacle in the treatment of clear cell renal cell carcinoma (ccRCC), yet the underlying mechanisms are poorly defined. Here, we identify a previously unrecognized axis involving Tribbles homolog 3 (TRIB3) and coactivator-associated arginine methyltransferase 1 (CARM1) that drives chemoresistance through modulation of Akt signaling. Mechanistically, TRIB3 directly interacts with CARM1, a pro-survival epigenetic regulator, and inhibits its ubiquitination to stabilize CARM1 protein levels. Elevated CARM1 further exacerbates therapeutic resistance, establishing a feedforward loop that sustains Akt activation. Our findings uncovering a novel TRIB3-CARM1-Akt axis as a central driver of sunitinib resistance. This study provides mechanistic insights into ccRCC chemoresistance and highlights therapeutic targeting of the TRIB3-CARM1 axis as a promising strategy to overcome treatment failure. - Source: PubMed
Publication date: 2025/04/15
Hu DanfeiFan XiaodongChen XiaodongLi MingyaoXiong HuacaiFan XiaoxiaoChen Feng - [This corrects the article DOI: 10.1016/j.omtn.2023.102063.]. - Source: PubMed
Publication date: 2025/04/10
Cheng YimingWang XiaochenHuang ShuyuZhang LiangLan BeiLi XuanyuanChen HaoLiu ZhenfengSu YijieXi LishanFeng ShengyunGuo YanxuanZhou JunWang YingmeiXuan Chenghao - [This corrects the article DOI: 10.1016/j.omton.2025.200952.]. - Source: PubMed
Publication date: 2025/03/28
Ni WeiGarg SwatiChowdhury BasudevSattler MartinSanchez DanaMeng ChengchengAkatsu TaiseiDonovan Katherine AQi JunWang Michelle YStarnbach Cara AnnLiu XiaoxiGuzman Maria TarazonaTeh Wei PinStone RichardGriffin James DBuhrlage SaraWeisberg Ellen