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First published online 10 February 2009
doi: 10.1242/jcs.039933

Journal of Cell Science 122, 667-677 (2009)
Published by The Company of Biologists 2009
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Research Article

Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Frank Herrmann1, Peter Pably2, Carmen Eckerich2, Mark T. Bedford3 and Frank O. Fackelmayer2,*

1 EMBL-CRG Systems Biology Research Unit, Centre for Genomic Regulation (CRG), c/Dr. Aiguader 88, 08003 Barcelona, Spain
2 Biomedical Research Institute, Foundation for Research and Technology Hellas, 45110 Ioannina, Greece
3 Department of Carcinogenesis, M. D. Anderson Cancer Center, University of Texas, 1808 Park Road 1C, Smithville, TX 78957, USA

* Author for correspondence (e-mail: frank{at}fackelmayer.de)

Accepted 17 November 2008

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.

Key words: Arginine methylation, Subcellular localization and dynamics, Posttranslational modification, Histone methylation, Epigenetics


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