Abstract
Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes ER stress. The ER stress sensor inositol requiring enzyme-1beta (IRE1β), which is specifically expressed in intestinal epithelial cells, is thought to be involved in translational repression. However, its mechanism of action is not fully understood. Using a reporter that can evaluate and distinguish between translation efficiency in the cytosol and on the ER membrane, we show here that IRE1β represses translation on the ER membrane but not in the cytosol, and that this selective repression depends on the RNase activity of IRE1β.
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blotting, Western
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Cytosol / metabolism
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Down-Regulation
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Endoplasmic Reticulum / metabolism*
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Endoribonucleases / genetics
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Endoribonucleases / metabolism*
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Glycoproteins / genetics
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Glycoproteins / metabolism
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HeLa Cells
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Humans
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Protein Biosynthesis*
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Protein Transport
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Reverse Transcriptase Polymerase Chain Reaction
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Ribonucleases / metabolism
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Secretory Pathway
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Stress, Physiological
Substances
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Glycoproteins
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Membrane Proteins
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RNA, Messenger
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ERN2 protein, human
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Protein Serine-Threonine Kinases
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Endoribonucleases
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Ribonucleases