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Methylation of Smad6 by protein arginine N ‐methyltransferase 1
Author(s) -
Inamitsu Masako,
Itoh Susumu,
Hellman Ulf,
ten Dijke Peter,
Kato Mitsuyasu
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.11.008
Subject(s) - methylation , methyltransferase , arginine , chemistry , biochemistry , biology , amino acid , dna
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.