| First Author | Inamitsu M | Year | 2006 |
| Journal | FEBS Lett | Volume | 580 |
| Issue | 28-29 | Pages | 6603-11 |
| PubMed ID | 17118358 | Mgi Jnum | J:201257 |
| Mgi Id | MGI:5512842 | Doi | 10.1016/j.febslet.2006.11.008 |
| Citation | Inamitsu M, et al. (2006) Methylation of Smad6 by protein arginine N-methyltransferase 1. FEBS Lett 580(28-29):6603-11 |
| abstractText | Signal transduction pathways utilize posttranslational modifications to regulate the activity of their components in a temporal-spatial and efficient fashion. Arginine methylation is one of the posttranslational modifications that can result in monomethylated-, asymmetric dimethylated- and/or symmetric dimethylated-arginine residues in proteins. Here we demonstrate that inhibitory-Smads (Smad6 and Smad7), but not receptor-regulated- (R-)Smads and the common-partner Smad4, can be methylated by protein arginine N-methyltransferase (PRMT)1. Using mass-spectrometric analysis, we found that PRMT1 dimethylates arginine(74) (Arg(74)) in mouse Smad6. PRMT1 interacts with the N-terminal domain of Smad6 in which Arg(74) residue is located. Assays examined so far have shown no significant differences between the functions of Smad6 and those of methylation-defective Smad6 (Smad6R74A). Both wild-type and Smad6R74A were equally efficient in blocking BMP-induced growth arrest upon their ectopic expression in HS-72 mouse B-cell hybridoma cells. |
