کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2052167 | 1543466 | 2006 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Methylation of Smad6 by protein arginine N-methyltransferase 1 Methylation of Smad6 by protein arginine N-methyltransferase 1](/preview/png/2052167.png)
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 arginine74 (Arg74) in mouse Smad6. PRMT1 interacts with the N-terminal domain of Smad6 in which Arg74 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.
Journal: FEBS Letters - Volume 580, Issues 28–29, 11 December 2006, Pages 6603–6611