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1. State Key Laboratory of Silkworm Genome Biology, Southwest University,Chongqing,China,400716
2. Cancer Center, Medical Research Institute, Southwest University,Chongqing,China,400716
3. Department of Gastroenterology, The Affiliated Hospital of Southwest Medical University, 25 Taiping Street, Jiangyang District,Sichuan,Luzhou,China,646000
4. Jinfeng Laboratory,Chongqing,China,401329
纸质出版日期:2023,
网络出版日期:2023-11-1,
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PRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway[J]. Genes & Diseases, 2023,1(6):2622-2638.
Feng Wang, Shitong Chen, Shihan Peng, et al. PRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway[J]. Genes & Diseases, 2023,1(6):2622-2638.
PRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway[J]. Genes & Diseases, 2023,1(6):2622-2638. DOI: 10.1016/j.gendis.2023.02.006.
Feng Wang, Shitong Chen, Shihan Peng, et al. PRMT1 promotes the proliferation and metastasis of gastric cancer cells by recruiting MLXIP for the transcriptional activation of the β-catenin pathway[J]. Genes & Diseases, 2023,1(6):2622-2638. DOI: 10.1016/j.gendis.2023.02.006.
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
in vitro
and
in vivo
. 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 between TRIM48 and PRMT1. Collectively
our findings reveal a mechanism by which PRMT1 promotes cell proliferation and metastasis mediated by the β-catenin signaling pathway.
β-catenin signaling pathwayGastric cancerPRMT1Transcriptional regulationUbiquitination
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