Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family.
Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. All members have been, to different degrees, characterized individually and their implication in cellular processes has been inferred from characterizing substrates and interactions. Here, we report the first comprehensive comparison of all eight canonical members of the human PRMT family with respect to subcellular localization and dynamics in living cells. We show that the individual family members differ significantly in their properties, as well as in their substrate specificities, suggesting that they fulfil distinctive, non-redundant functions in vivo. In addition, certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions.
Herrmann
Frank
F
EMBL-CRG Systems Biology Research Unit, Centre for Genomic Regulation (CRG), c/Dr. Aiguader 88, 08003 Barcelona, Spain.
Pably
Peter
P
Eckerich
Carmen
C
Bedford
Mark T
MT
Fackelmayer
Frank O
FO
D002460:Cell Line; D036681:Fluorescence Recovery After Photobleaching; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
D007527:Isoenzymes; D011993:Recombinant Fusion Proteins; D011484:Protein-Arginine N-Methyltransferases