Ask about this productRelated genes to: PCIF1 antibody
- Gene:
- PCIF1 NIH gene
- Name:
- PDX1 C-terminal inhibiting factor 1
- Previous symbol:
- C20orf67
- Synonyms:
- bA465L10.1, PPP1R121
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-17
- Date modifiied:
- 2014-11-19
Related products to: PCIF1 antibody
Related articles to: PCIF1 antibody
- Phosphorylated CTD-interacting factor 1 (PCIF1) has been recently discovered to introduce a methyl group at the N6 position of the first transcribed Am-adenosine in nascent capped mRNA (mAm modification), modulating mRNA stability, transcription, and translation. In addition, the activity of PCIF1 is involved in various diseases, making PCIF1 a potential therapeutic target. In the absence of complete crystal structures of PCIF1 with an RNA substrate and/or cofactor and with the aim of accessing potent inhibitors, the bisubstrate strategy was employed to synthesize a series of bisubstrate analogs of PCIF1 that contain an analog of the cofactor S-adenosyl-L-methionine (SAM) covalently linked to an Am-modified RNA substrate. The versatility of the synthesis was exploited to increase structural diversity at the amino acid chain of SAM, and a cap analog was introduced by click chemistry. Also, AlphaFold 3 was used to generate a complete structure of PCIF1 with an RNA substrate. Docking studies carried out with the bisubstrates indicate that the SAM analog occupies the cofactor binding site while the Am-RNA substrate interacts with the putative RNA pocket. We think that these results could be a valuable starting point for the design of potent inhibitors of PCIF1. - Source: PubMed
Publication date: 2026/04/09
Colas YoannLe Corre LaurentEthève-Quelquejeu MélanieBraud Emmanuelle - Osteogenesis depends on the self-renewal and differentiation of mesenchymal stem cells (MSCs). Emerging research underscores the regulatory functions of RNA methylation on bone homeostasis. Here, we show PCIF1, the N6,2'-O-dimethyladenosine (m6Am) methyltransferase, is essential for maintaining bone mass and promoting osteogenic differentiation of MSCs. Multiple complementary analyses-including GWAS, TWAS, and single-cell transcriptomics-collectively point to PCIF1 as a regulator of human bone mineral traits and early-stage mesenchymal differentiation. Global or MSC-specific Pcif1 deletion elicits osteoporotic pathology in mice, although myeloid cell-specific Pcif1 knockout does not induce femur bone alterations. Mechanistically, Pcif1 knockout decreases m6Am signals of Wnt-related genes (Wnt11, Fzd4, and Fgfr2) and accelerates mRNA degradation. This down-regulates active β-Catenin protein, and thus impairs osteogenic function of MSCs. Additionally, the WNT agonist attenuates the osteoporosis-like phenotype induced by Pcif1 deletion. These findings highlight the crucial role of PCIF1-mediated m6Am modification in regulating osteogenesis and suggest potential therapeutic implications for bone disorders. - Source: PubMed
Publication date: 2026/04/06
Song WeiSu Kuan-JuiPan ZhehuiZhang ZhongYin QiLin WeiminLiu LinfengGong YunLiang BochengCai YimengLi QiwenShen HuiDeng Hong-WenYuan Quan - N,2'-O-dimethyladenosine (mAm) is a prevalent RNA modification located at the first transcribed nucleotide adjacent to the 5' cap of mRNAs, where it has been implicated in gene regulation. However, the lack of methods for precise, transcript-specific manipulation of mAm has limited its functional dissection. Here, we develop a programmable RNA-editing platform, termed Targeted mAm Methylation (TAmM), that enables site-specific installation of mAm on selected cellular transcripts. TAmM is engineered by fusing the catalytically inactive RfxCas13d (dCasRx) with the mAm methyltransferase PCIF1, allowing guided deposition of mAm at cap-proximal nucleotides. Using TAmM, we achieve efficient and specific mAm installation at single-nucleotide resolution, as validated by LC-MS/MS. Targeted mAm editing does not alter steady-state mRNA abundance but modulates protein output in a transcript-dependent manner. Mechanistically, mAm installation enhances polysome association, indicating a direct role in translational regulation. Functional interrogation demonstrates that cap-proximal mAm deposition on CTNNB1 increases β-catenin protein expression, promoting cell proliferation, clonogenicity, and migration in cancer cell models. Importantly, TAmM exhibits high fidelity, with negligible effects on the global mAm landscape, transcriptome, or proteome. Our study establishes TAmM as a precise and versatile platform for programmable mAm manipulation and reveals transcript-specific roles of mAm in gene regulation. - Source: PubMed
Publication date: 2026/03/13
Li YangTan XiangminLiu YaranHe YongquanYuan BoWang PingMa GuangzhiGuo MengzheZhou JianSun Qiang - Polycystic ovary syndrome (PCOS) is a prevalent endocrine disorder, the molecular underpinnings of which remain largely undefined. The most common methylation modification of RNA, N-methyladenosine (m6A), plays an important role in various reproductive and endocrine disorders. This study investigates key m6A genes in PCOS and their association with immune cell infiltration using advanced bioinformatics methods. - Source: PubMed
Xu WentingShi LingliLu AifangCui LijuanQian HaiqingWang JiahuiTang MengyuZhu LiliWang Lihong - N6,2'-O-dimethyladenosine (mAm) modification, mediated by the methyltransferase phosphorylated CTD interacting factor 1 (PCIF1), is increasingly recognized as an important layer of gene regulation. However, the role of mAm in pain and comorbid anxiety has not yet been explored. Here, we report that persistent peripheral inflammation reduces PCIF1 levels in the mouse anterior cingulate cortex (ACC). This downregulation is triggered by decreased binding of GLI2 to the Pcif1 promoter. Knocking out or conditionally deleting Pcif1 in ACC neurons reduces the mAm level of Gap43 mRNA, leading to the increased expression of GAP43 and pre-long-term potentiation (LTP) oversaturation, which in turn results in inflammatory pain and its comorbid anxiety-like behavior. Conversely, knocking down GAP43 suppresses the pre-LTP oversaturation caused by PCIF1 reduction, thereby alleviating inflammatory pain and comorbid anxiety. This study reveals a mechanism whereby GLI2-governed PCIF1 contributes to the modulation of inflammatory pain and comorbid anxiety through the targeting of Gap43 mAm in the ACC. - Source: PubMed
Publication date: 2026/02/18
Liu YaHuang YueXue KeqingMa GanXie ShanZhao YaxuanZeng YingLi ShuangshuangYang LiHao LingyunZhao XiaotianWang HongjunWang QihuiWang CunjinPan Zhiqiang