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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5453
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pubmed:dateCreated |
2000-2-18
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pubmed:abstractText |
Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and IRE1alpha-/- fibroblasts were impaired in JNK activation by ER stress. The cytoplasmic part of IRE1 bound TRAF2, an adaptor protein that couples plasma membrane receptors to JNK activation. Dominant-negative TRAF2 inhibited activation of JNK by IRE1. Activation of JNK by endogenous signals initiated in the ER proceeds by a pathway similar to that initiated by cell surface receptors in response to extracellular signals.
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pubmed:grant |
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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/ERN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Ern2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PERK kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-2 Kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
287
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
664-6
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pubmed:dateRevised |
2010-5-21
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pubmed:meshHeading |
pubmed-meshheading:10650002-Animals,
pubmed-meshheading:10650002-Cell Line,
pubmed-meshheading:10650002-Cells, Cultured,
pubmed-meshheading:10650002-Endoplasmic Reticulum,
pubmed-meshheading:10650002-Endoribonucleases,
pubmed-meshheading:10650002-Enzyme Activation,
pubmed-meshheading:10650002-Gene Targeting,
pubmed-meshheading:10650002-Humans,
pubmed-meshheading:10650002-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:10650002-Membrane Proteins,
pubmed-meshheading:10650002-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10650002-Protein Kinases,
pubmed-meshheading:10650002-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10650002-Proteins,
pubmed-meshheading:10650002-Rats,
pubmed-meshheading:10650002-Recombinant Fusion Proteins,
pubmed-meshheading:10650002-TNF Receptor-Associated Factor 2,
pubmed-meshheading:10650002-Thapsigargin,
pubmed-meshheading:10650002-Two-Hybrid System Techniques,
pubmed-meshheading:10650002-eIF-2 Kinase
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pubmed:year |
2000
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pubmed:articleTitle |
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
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pubmed:affiliation |
Skirball Institute of Biomolecular Medicine, Departments of Medicine, Cell Biology and the Kaplan Cancer Center, New York University Medical School, New York, NY 10016, USA.
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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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