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Methylation of Smad6 by protein arginine N-methyltransferase 1
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
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2006 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 28-29, 6603-6611 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2006. Vol. 580, no 28-29, 6603-6611 p.
Keyword [en]
BMP, I-Smad, PRMT1, Smad6, Smad7
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-146979DOI: 10.1016/j.febslet.2006.11.008ISI: 000242946200013PubMedID: 17118358OAI: oai:DiVA.org:uu-146979DiVA: diva2:399520
Available from: 2011-02-22 Created: 2011-02-22 Last updated: 2011-02-28Bibliographically approved

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