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A more recent version of this article appeared on September 1, 2003
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Submitted on January 3, 2003
Accepted on April 27, 2003
1 Department of Molecular Biology, University of Medicine and Dentistry New Jersey- School of Osteopathic Medicine, Stratford, NJ 08084, USA
* Corresponding author. E-mail address: henrymf{at}umdnj.edu.
The Hrp1/Nab4 shuttling protein belongs to a family of RNA binding proteins that bind to nascent RNA polymerase II transcripts and form hnRNP complexes. Members of this family function in a staggering array of cellular activities, ranging from transcription and premRNA processing in the nucleus to cytoplasmic mRNA translation and turnover. It has recently been recognized that the yeast stress response can include alterations in hnRNP-mediated mRNA export. We now report that the steady state localization of Hrp1p rapidly shifts from the nucleus to the cytoplasm in response to osmotic stress. In contrast to a general stress response resulting in a transient relocation, Hrp1p redistribution is specific to hyperosmotic stress, and is only reversed following stress removal. Hrp1p relocalization requires both the CRM1/XPO1 exportin and the FPS1 glycerol transporter genes but is independent of ongoing RNA transcription and protein arginine methylation. However, mutations in the high osmolarity glycerol (HOG) and protein kinase C (PKC) osmosensing pathways do not impact the Hrp1p hyperosmotic response. We will present a working model for the cytoplasmic accumulation of Hrp1 and discuss the implications of this relocalization on Hrp1p function.
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