HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Herrmann, F. Articles by Fackelmayer, F. O. Search for Related Content PubMed Articles by Herrmann, F. Articles by Fackelmayer, F. O.

¹ EMBL-CRG Systems Biology, c/Doctor Aiguader 88, 08003 Barcelona, Spain
² Biomedical Research Institute, Foundation for Research and Technology Hellas, 45110 Ioannina, Greece

Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMT), of which PRMT1 is the predominant member in human cells. We have previously described the localization and mobility of PRMT1 in live cells, and found that it shuttles between the nucleus and the cytoplasm depending on the methylation status of substrate proteins. Recently, amino-terminal splicing isoforms of PRMT1 were shown to differ significantly in intracellular localization, the most interesting being splice variant 2 that carries a nuclear export signal in its amino terminus, and is expressed in increased levels in breast cancer cells. We show here that enzymatic activity is required for nucleo-cytoplasmic shuttling of PRMT1v2, as a catalytically inactive mutant highly accumulates in the nucleus and displays altered intranuclear mobility as determined by fluorescence recovery after photobleaching experiments. Our results indicate that nuclear export of PRMT1v2 is dominant over activity-independent nuclear import, but can only occur after activity-dependent release of the enzyme from substrates, suggesting that shuttling of the enzyme provides a dynamic mechanism for the regulation of substrate methylation.

^* Correspondence: frank{at}fackelmayer.de

This article has been cited by other articles:

				F. Herrmann, P. Pably, C. Eckerich, M. T. Bedford, and F. O. Fackelmayer Human protein arginine methyltransferases in vivo - distinct properties of eight canonical members of the PRMT family J. Cell Sci., March 1, 2009; 122(5): 667 - 677. [Abstract] [Full Text] [PDF]