Protein arginine methyltransferase 1 interacts with Gli1 and regulates its transcriptional activity
Tumor Biology, ISSN: 1423-0380, Vol: 37, Issue: 7, Page: 9071-9076
2016
- 7Citations
- 8Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations7
- Citation Indexes7
- CrossRef5
- Captures8
- Readers8
Article Description
Protein arginine methylation, which is mediated by the protein arginine methyltransferases (PRMTs), is associated with numerous fundamental cellular processes. Our previous studies have shown that PRMT1 activated Hedgehog signaling in the esophageal squamous cell carcinoma (ESCC) cells and promoted the growth and migration of cancer cells. However, the detailed mechanisms are unknown. In this study, it was found that PRMT1 interacted with the transcriptional factor Gli1 (glioma-associated oncogene homolog 1) in ESCC cells. The DNA-binding domain (DBD) of Gli1 is responsible for its interaction with PRMT1. Moreover, PRMT1 promoted the methylation of Gli1, and knocking down the expression of PRMT1 impaired the transcriptional activity as well as the biological functions of Gli1. Taken together, our study demonstrated that PRMT1 is a positive regulator of Hedgehog signaling, and PRMT1 might be a therapeutic target for ESCC.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84954316954&origin=inward; http://dx.doi.org/10.1007/s13277-015-4754-7; http://www.ncbi.nlm.nih.gov/pubmed/26762411; http://link.springer.com/10.1007/s13277-015-4754-7; https://dx.doi.org/10.1007/s13277-015-4754-7; https://link.springer.com/article/10.1007/s13277-015-4754-7
Springer Science and Business Media LLC
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