biostudies-literatureWang FNatural Science Foundation of Chongqing MunicipalityNatural Science Foundation Project of ChongqingPostdoctoral Research Foundation of ChinaNational Natural Science Foundation of ChinaChongqing Postdoctoral Science Foundation2622-2638https://www.ebi.ac.uk/biostudies/studies/S-EPMC10404965biostudies-literatureUnknown10(6)Protein arginine methyltransferase 1 (PRMT1), a type I PRMT, is overexpressed in gastric cancer (GC) cells. To elucidate the function of PRMT1 in GC, PRMT1 expression in HGC-27 and MKN-45 cells was knocked down by short hairpin RNA (shRNA) or inhibited by PRMT1 inhibitors (AMI-1 or DCLX069), which resulted in inhibition of GC cell proliferation, migration, invasion, and tumorigenesis <i>in vitro</i> and <i>in vivo</i>. MLX-interacting protein (MLXIP) and Kinectin 1 (KTN1) were identified as PRMT1-binding proteins. PRMT1 recruited MLXIP to the promoter of β-catenin, which induced β-catenin transcription and activated the β-catenin signaling pathway, promoting GC cell migration and metastasis. Furthermore, KTN1 inhibited the K48-linked ubiquitination of PRMT1 by decreasing the interaction beGenes & diseasesPRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway.PMC10404965cstc2022ycjh-bgzxm0145cstc2021jcyj-bsh00678220333978201006072021M692679Yang HKe XLu MLiang HPeng SWang FCui HZhong XChen SZhou XTang HfalsePRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway.Protein arginine methyltransferase 1 (PRMT1), a type I PRMT, is overexpressed in gastric cancer (GC) cells. To elucidate the function of PRMT1 in GC, PRMT1 expression in HGC-27 and MKN-45 cells was knocked down by short hairpin RNA (shRNA) or inhibited by PRMT1 inhibitors (AMI-1 or DCLX069), which resulted in inhibition of GC cell proliferation, migration, invasion, and tumorigenesis <i>in vitro</i> and <i>in vivo</i>. MLX-interacting protein (MLXIP) and Kinectin 1 (KTN1) were identified as PRMT1-binding proteins. PRMT1 recruited MLXIP to the promoter of β-catenin, which induced β-catenin transcription and activated the β-catenin signaling pathway, promoting GC cell migration and metastasis. Furthermore, KTN1 inhibited the K48-linked ubiquitination of PRMT1 by decreasing the interaction be2023-01-01T00:00:00Z2023 Nov2025-04-05T14:51:49.203Z2025-04-05T14:51:49.203ZS-EPMC104049653755421810.1016/j.gendis.2023.02.006