Journal
FASEB JOURNAL
Volume 31, Issue 6, Pages 2287-2300Publisher
FEDERATION AMER SOC EXP BIOL
DOI: 10.1096/fj.201601196R
Keywords
migration; invasion; E-cadherin; YY1
Categories
Funding
- Natural Science Foundation of China [31570718, 31571317, 31571478, 31401105, 31371294]
- Jilin Scientific and Technological Development Program [20140520003JH]
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Protein arginine methyltransferases (PRMTs) catalyze protein arginine methylation and are linked to carcinogenesis and metastasis. Some members of PRMTs have been found to undergo automethylation; however, the biologic significance of this self-modification is not entirely clear. In this report, we demonstrate that R531 of PRMT7 is self-methylated, both in vitro and in vivo. Automethylation of PRMT7 plays a key role in inducing the epithelial-mesenchymal transition (EMT) program and in promoting the migratory and invasive behavior of breast cancer cells. We also prove in a nude mouse model that expression of wild-type PRMT7 in MCF7 breast cancer cells promotes metastasis in vivo, in contrast to the PRMT7 R531K mutant (a mimic of the unmethylated status). Moreover, our immunohistochemical data unravel a close link between PRMT7 automethylation and the clinical outcome of breast carcinomas. Mechanistically, we determine that loss of PRMT7 automethylation leads to the reduction of its recruitment to the E-cadherin promoter by YY1, which consequently derepresses the E-cadherin expression through decreasing the H4R3me2s level. The findings in this work define a novel post-translational modification of PRMT7 that has a promoting impacton breast cancer metastasis.
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