| First Author | Goulet I | Year | 2007 |
| Journal | J Biol Chem | Volume | 282 |
| Issue | 45 | Pages | 33009-21 |
| PubMed ID | 17848568 | Mgi Jnum | J:127017 |
| Mgi Id | MGI:3762605 | Doi | 10.1074/jbc.M704349200 |
| Citation | Goulet I, et al. (2007) Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization. J Biol Chem 282(45):33009-21 |
| abstractText | PRMT1 is the predominant member of a family of protein arginine methyltransferases (PRMTs) that have been implicated in various cellular processes, including transcription, RNA processing, and signal transduction. It was previously reported that the human PRMT1 pre-mRNA was alternatively spliced to yield three isoforms with distinct N-terminal sequences. Close inspection of the genomic organization in the 5'-end of the PRMT1 gene revealed that it can produce up to seven protein isoforms, all varying in their N-terminal domain. A detailed biochemical characterization of these variants revealed that unique N-terminal sequences can influence catalytic activity as well as substrate specificity. In addition, our results uncovered the presence of a functional nuclear export sequence in PRMT1v2. Finally, we find that the relative balance of PRMT1 isoforms is altered in breast cancer. |
