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Nucleic Acids Research 2005 33(4):1309-1322; doi:10.1093/nar/gki269
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Published online 1 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

A family of RS domain proteins with novel subcellular localization and trafficking

Steven J. Kavanagh1,2, Thomas C. Schulz1,2, Philippa Davey1,2, Charles Claudianos3, Carrie Russell1 and Peter D. Rathjen1,2,4,*

1School of Molecular and Biomedical Science, University of Adelaide Adelaide 5005, Australia 2Australian Research Council Special Research Centre in Molecular Genetics, University of Adelaide Adelaide 5005, Australia 3Molecular Genetics and Evolution, Research School of Biological Sciences, Australian National University ACT 2601, Australia 4National Stem Cell Centre Notting Hill, VIC 3168, Australia

*To whom correspondence should be addressed. Tel: +61 8 8303 5650; Fax: +61 8 8303 4348; Email: peter.rathjen{at}adelaide.edu.au

Received September 7, 2004. Revised December 23, 2004. Accepted February 8, 2005.

We report the sequence, conservation and cell biology of a novel protein, Psc1, which is expressed and regulated within the embryonic pluripotent cell population of the mouse. The Psc1 sequence includes an RS domain and an RNA recognition motif (RRM), and a sequential arrangement of protein motifs that has not been demonstrated for other RS domain proteins. This arrangement was conserved in a second mouse protein (BAC34721. The identification of Psc1 and BAC34721homologues in vertebrates and related proteins, more widely throughout evolution, defines a new family of RS domain proteins termed acidic rich RS (ARRS) domain proteins. Psc1 incorporated into the nuclear speckles, but demonstrated novel aspects of subcellular distribution including localization to speckles proximal to the nuclear periphery and localization to punctate structures in the cytoplasm termed cytospeckles. Integration of Psc1 into cytospeckles was dependent on the RRM. Cytospeckles were dynamic within the cytoplasm and appeared to traffic into the nucleus. These observations suggest a novel role in RNA metabolism for ARRS proteins.

DDBJ/EMBL/GenBank accession no.+

+AY461716


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