Arginine methylation of hnRNP A2 does not directly govern its subcellular localization

Friend, Lexie R., Landsberg, Michael J., Nouwens, Amanda S., Wei, Ying, Rothnagel, Joseph A. and Smith, Ross (2013) Arginine methylation of hnRNP A2 does not directly govern its subcellular localization. PLoS One, 8 9: e75669.1-e75669.12. doi:10.1371/journal.pone.0075669

Author Friend, Lexie R.
Landsberg, Michael J.
Nouwens, Amanda S.
Wei, Ying
Rothnagel, Joseph A.
Smith, Ross
Title Arginine methylation of hnRNP A2 does not directly govern its subcellular localization
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2013-09-30
Year available 2013
Sub-type Article (original research)
DOI 10.1371/journal.pone.0075669
Open Access Status DOI
Volume 8
Issue 9
Start page e75669.1
End page e75669.12
Total pages 12
Editor Wei-Guo Zhu
Place of publication San Francisco, United States
Publisher Public Library of Science
Collection year 2014
Language eng
Formatted abstract
The hnRNP A/B paralogs A1, A2/B1 and A3 are key components of the nuclear 40S hnRNP core particles. Despite a high degree of sequence similarity, increasing evidence suggests they perform additional, functionally distinct roles in RNA metabolism. Here we identify and study the functional consequences of differential post-translational modification of hnRNPs A1, A2 and A3. We show that while arginine residues in the RGG box domain of hnRNP A1 and A3 are almost exhaustively, asymmetrically dimethylated, hnRNP A2 is dimethylated at only a single residue (Arg-254) and this modification is conserved across cell types. It has been suggested that arginine methylation regulates the nucleocytoplasmic distribution of hnRNP A/B proteins. However, we show that transfected cells expressing an A2R254A point mutant exhibit no difference in subcellular localization. Similarly, immunostaining and mass spectrometry of endogenous hnRNP A2 in transformed cells reveals a naturally-occurring pool of unmethylated protein but an exclusively nuclear pattern of localization. Our results suggest an alternative role for post-translational arginine methylation of hnRNPs and offer further evidence that the hnRNP A/B paralogs are not functionally redundant.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
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Created: Fri, 04 Oct 2013, 11:01:07 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences