AI Article Synopsis
- Signal transduction pathways use posttranslational modifications like arginine methylation to regulate protein activity efficiently and in a targeted manner.
- In this study, it's shown that inhibitory Smads (Smad6 and Smad7) can be methylated by PRMT1, specifically focusing on the dimethylation of arginine 74 in mouse Smad6.
- Experiments indicate that methylation of Smad6 does not significantly alter its function, as both methylated and non-methylated forms effectively block BMP-induced growth arrest in specific mouse B-cell hybridoma cells.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.febslet.2006.11.008 | DOI Listing |
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