The overexpression of certain membrane proteins is accompanied by a striking proliferation of intracellular membranes. One of the best characterized inducers of membrane proliferation is the 180-kD mammalian ribosome receptor (p180), whose expression in yeast results in increases in levels of mRNAs encoding proteins that function in the secretory pathway, and an elevation in the cell's ability to secrete proteins. In this study we demonstrate that neither the unfolded protein response nor increased transcription accounts for membrane proliferation or the observed increase in secretory pathway mRNAs. Rather, p180-induced up-regulation of certain secretory pathway transcripts is due to a p180-mediated increase in the longevity of these mRNA species, as determined by measurements of transcriptional activity and specific mRNA turnover. Moreover, we show that the longevity of mRNA in general is substantially promoted through the process of its targeting to the membrane of the endoplasmic reticulum. With respect to the terminal differentiation of secretory tissues, results from this model system provide insights into how the expression of a single protein, p180, could result in substantial morphological and functional changes.
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18 March 2002
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March 18 2002
Induction of secretory pathway components in yeast is associated with increased stability of their mRNA
Maureen Hyde,
Maureen Hyde
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
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Laura Block-Alper,
Laura Block-Alper
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
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Jahaira Felix,
Jahaira Felix
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
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Paul Webster,
Paul Webster
2Ahmanson Center for Advanced EM and Imaging, House Ear Institute, Los Angeles, CA 90057
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David I. Meyer
David I. Meyer
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
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Maureen Hyde
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
Laura Block-Alper
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
Jahaira Felix
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
Paul Webster
2Ahmanson Center for Advanced EM and Imaging, House Ear Institute, Los Angeles, CA 90057
David I. Meyer
1Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, and the Molecular Biology Institute, Los Angeles, CA 90024
Address correspondence to David I. Meyer, Department of Biological Chemistry, University of California at Los Angeles School of Medicine, Los Angeles, CA 90024-1737. Tel.: (310) 206-3122. Fax: (310) 206-5197. E-mail: [email protected]
M. Hyde and L. Block-Alper contributed equally to this work.
*
Abbreviations used in this paper: FP, free polysomes; GFP, green fluorescent protein; MBP, membrane-bound polysomes; UPR, unfolded protein response.
Received:
December 03 2001
Revision Received:
January 16 2002
Accepted:
February 05 2002
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2002
J Cell Biol (2002) 156 (6): 993–1001.
Article history
Received:
December 03 2001
Revision Received:
January 16 2002
Accepted:
February 05 2002
Citation
Maureen Hyde, Laura Block-Alper, Jahaira Felix, Paul Webster, David I. Meyer; Induction of secretory pathway components in yeast is associated with increased stability of their mRNA . J Cell Biol 18 March 2002; 156 (6): 993–1001. doi: https://doi.org/10.1083/jcb.200112008
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