Fig 2: A hypothetical model of PRMT1 and SMARCA4 regulating cell proliferation and CRC progression

Fig 3: The methyltransferase activity of PRMT1 is essential for adipocyte differentiation.A, 3T3-L1 cells were treated with vehicle (DMSO) or 0.5, 1, and 2 µM TC-E5003 for 36 h and then subjected to Western blot analyses using the corresponding antibodies. B, oil red O (ORO) staining of differentiated 3T3-L1 cells treated with vehicle (DMSO) or 0.5, 1, and 2 µM TC-E5003. The scale bar represents 200 µm. C, absorption of the eluate was measured photometrically at 510 nm for ORO. Data are shown as mean ± SD (n = 3). Student’s t test, n.s. not significance, *p < 0.05, **p < 0.01. D, relative mRNA levels of adipogenic marker genes in differentiated 3T3-L1 cells with the treatment of vehicle (DMSO) or 0.5, 1, and 2 µM TC-E5003 at day 6. Results are shown as mean ± SD (n = 3). Student’s t test, *p < 0.05, **p < 0.01, ***p < 0.001. E, the protein levels of C/EBPa and PPAR? as indicated in (D). ß-tubulin serves as the internal reference. F, qPCR analysis of C/EBPa, PPAR?, and FABP4 in C3H10T1/2 cells with or without TC-E 5003 (2 µM) after induction of adipocyte differentiation for 6 days. Data are presented as mean ± SD (n = 3). Student’s t test, ***p < 0.001. G, Bodipy staining determined the adipogenic phenotypes of C3H10T1/2 cells treated with DMSO or TC-E 5003 (2 µM) after DMI induction for 6 days. The scale bar represents 200 µm. H, the quantification of Bodipy positive cells. Presented as mean ± SD (n = 3). Student’s t test, ***p < 0.001. DMSO, dimethyl sulfoxide; qPCR, quantitative PCR.

Fig 4: Proteins involved in RNA metabolism emerge as preferential PRMT1 substrates and binding partners.a Analysis of PTMScan data from PATC53 cells treated with 1 µM PRMTi or DMSO control for 24 h. Enrichment analysis for gene ontology (GO) biological processes were conducted using Fisher’s exact test for proteins with MMA enrichment upon treatment vs. all proteins analyzed. The x-axis indicates the ratio of enriched vs. total genes analyzed per GO term. Dashed lines indicate FDR-adjusted significance thresholds at q = 0.05 and q = 0.01. GO terms associated with RNA splicing or processing highlighted in red, and four of the five splicing/processing sets were enriched with q < 0.05. b PRMT1 Western Blot (left) and Silver Staining (right) images of proteins isolated from PATC53 cells (input) and immunoprecipitated with anti-IgG or anti-PRMT1 antibodies. The red square denotes PRMT1 protein. c Enrichment analysis of PRMT1 IP-MS data in PATC53 cells. RNA processing and splicing terms are denoted with red points, all others are black. Dashed lines indicate FDR-adjusted significance thresholds at q = 0.05, q = 0.01, and q = 0.001. Eight of eleven RNA processing/splicing terms are enriched with q < 0.05. d PTMScan MMA analysis (yellow) shows enrichment of RNA processing gene sets, many of which are supported by both IP-MS and PTMScan data (red). Source data are provided as a Source Data file.

Fig 5: FUS/TLS and PRMT1 are partially co-localized in SGs in SH-SY5Y cells.SH-SY5Y cells were exposed to mock (A) or 0.5 mM arsenite (B) for 30 minutes, then co-stained with indicated antibodies and followed by the incubation with fluorescence conjugated secondary antibody. Samples were then stained with DAPI. Images were obtained using fluorescence microscopy. Bars, 20 µm. Arrows indicate the co-localizations.