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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-2-14
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pubmed:abstractText |
Unfolded or misfolded proteins in the endoplasmic reticulum (ER) must be refolded or degraded to maintain homeostasis of the ER. The ATF6 and IRE1-XBP1 pathways are important for the refolding process in mammalian cells; activation of these transcriptional programs culminates in induction of ER-localized molecular chaperones and folding enzymes. We show here that degradation of misfolded glycoprotein substrates requires transcriptional induction of EDEM (ER degradation-enhancing alpha-mannosidase-like protein), and that this is mediated specifically by IRE1-XBP1 and not by ATF6. As XBP1 is produced after ATF6 activation, our results reveal a time-dependent transition in the mammalian unfolded protein response: an ATF6-mediated unidirectional phase (refolding only) is followed by an XBP1-mediated bidirectional phase (refolding plus degradation) as the response progresses.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATF6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Activating Transcription Factor 6,
http://linkedlifedata.com/resource/pubmed/chemical/Atf6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EDEM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ERN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Edem1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Ern2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/regulatory factor X transcription...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1534-5807
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-71
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pubmed:dateRevised |
2008-9-5
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pubmed:meshHeading |
pubmed-meshheading:12586069-Activating Transcription Factor 6,
pubmed-meshheading:12586069-Animals,
pubmed-meshheading:12586069-Blotting, Western,
pubmed-meshheading:12586069-DNA-Binding Proteins,
pubmed-meshheading:12586069-Endoplasmic Reticulum,
pubmed-meshheading:12586069-Endoribonucleases,
pubmed-meshheading:12586069-Gene Expression Regulation,
pubmed-meshheading:12586069-Genes, MHC Class II,
pubmed-meshheading:12586069-Glycoproteins,
pubmed-meshheading:12586069-HeLa Cells,
pubmed-meshheading:12586069-Humans,
pubmed-meshheading:12586069-Immunoblotting,
pubmed-meshheading:12586069-Luciferases,
pubmed-meshheading:12586069-Mannosidases,
pubmed-meshheading:12586069-Membrane Proteins,
pubmed-meshheading:12586069-Mice,
pubmed-meshheading:12586069-Mice, Knockout,
pubmed-meshheading:12586069-Protein Folding,
pubmed-meshheading:12586069-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12586069-Signal Transduction,
pubmed-meshheading:12586069-Transcription Factors,
pubmed-meshheading:12586069-Transfection
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pubmed:year |
2003
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pubmed:articleTitle |
A time-dependent phase shift in the mammalian unfolded protein response.
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pubmed:affiliation |
Graduate School of Biostudies, Kyoto University, Kyoto 606-8304, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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