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Nucleic Acids Research Advance Access published online on December 5, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm556
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Nuclear RNA export factor 7 is localized in processing bodies and neuronal RNA granules through interactions with shuttling hnRNPs

Jun Katahira1,2,*, Takashi Miki1, Keizo Takano1, Mitsuji Maruhashi3, Masanori Uchikawa3, Taro Tachibana4 and Yoshihiro Yoneda1,2

1Biomolecular Networks Laboratories, Biomolecular Dynamics Laboratory, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, 2Department of Cell Biology and Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, 3Developmental Biology Laboratory, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871 and 4Department of Bioengineering, Graduate School of Engineering, Osaka City University, Osaka 558-8585, Japan

To whom correspondence should be addressed. Tel: +81 6 6879 4606; Fax: +81 6 6879 4609; Email: katahira{at}anat3.med.osaka-u.ac.jp Correspondence may also be addressed to Yoshihiro Yoneda. Tel: +81 6 6879 4605, Fax: +81 6 6879 4609, Email: yyoneda{at}anat3.med.osaka-u.ac.jp Correspondence may also be addressed to Yoshihiro Yoneda. +81 6 6879 4605, +81 6 6879 4609, yyoneda{at}anat3.med.osaka-u.ac.jp

Received April 28, 2007. Revised June 25, 2007. Accepted July 6, 2007.

The nuclear RNA export factor (NXF) family proteins have been implicated in various aspects of post-transcriptional gene expression. This study shows that mouse NXF7 exhibits heterologous localization, i.e. NXF7 associates with translating ribosomes, stress granules (SGs) and processing bodies (P-bodies), the latter two of which are believed to be cytoplasmic sites of storage, degradation and/or sorting of mRNAs. By yeast two-hybrid screening, a series of heterogeneous nuclear ribonucleoproteins (hnRNPs) were identified as possible binding partners for NXF7. Among them, hnRNP A3, which is believed to be involved in translational control and/or cytoplasmic localization of certain mRNAs, formed a stable complex with NXF7 in vitro. Although hnRNP A3 was not associated with translating ribosomes, it was co-localized with NXF7 in P-bodies. After exposing to oxidative stress, NXF7 trans-localized to SGs, whereas hnRNP A3 did not. In differentiated neuroblastoma Neuro2a cells, NXF7 was co-localized with hnRNP A3 in cell body and neurites. The amino terminal half of NXF7, which was required for stable complex formation with hnRNP A3, coincided with the region required for localization in both P-bodies and neuronal RNA granules. These findings suggest that NXF7 plays a role in sorting, transport and/or storage of mRNAs through interactions with hnRNP A3.


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