FAM98A is a novel substrate of PRMT1 required for tumor cell migration, invasion, and colony formation
| Autor: | Khondker Ayesha Akter, Mohammed A. Mansour, Michinari Hamaguchi, Takeshi Senga, Satoko Ito, Toshinori Hyodo |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Protein-Arginine N-Methyltransferases Methyltransferase Arginine FAM98A Mice Nude Biology Methylation 03 medical and health sciences Cell Movement In vivo Cell Line Tumor medicine Animals Humans Neoplasm Invasiveness Proteins Cancer General Medicine medicine.disease Repressor Proteins HEK293 Cells 030104 developmental biology Cell culture Immunology Cancer research Ovarian cancer Protein Processing Post-Translational Neoplasm Transplantation |
| Zdroj: | Tumor Biology. 37:4531-4539 |
| ISSN: | 1423-0380 1010-4283 |
| DOI: | 10.1007/s13277-015-4310-5 |
| Popis: | Protein arginine methylation, which is mediated by a family of protein arginine methyltransferases (PRMTs), is associated with numerous fundamental cellular processes. Accumulating studies have revealed that the expression of multiple PRMTs promotes cancer progression. In this study, we examined the role of PRMT1 in ovarian cancer cells. PRMT1 is expressed in multiple ovarian cancer cells, and the depletion of its expression suppressed colony formation, in vivo proliferation, migration, and invasion. To gain insight into PRMT1-mediated cancer progression, we searched for novel substrates of PRMT1. We found that FAM98A, whose physiological function is unknown, was arginine-methylated by PRMT1. FAM98A is expressed in numerous ovarian cancer cell lines and is important for the malignant characteristics of ovarian cancer cells. Our results indicate the possible role of the PRMT1-FAM98A pathway in cancer progression. |
| Databáze: | OpenAIRE |
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