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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2010-3-26
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pubmed:abstractText |
Cells possess mechanisms that permit survival and recovery from stress, several of which regulate the phosphorylation of eukaryotic translation initiation factor 2alpha (eIF2alpha). We identified the human OGFOD1 protein as a novel stress granule component that regulates the phosphorylation of eIF2alpha and the resumption of translation in cells recovering from arsenite-induced stress. Coimmunoprecipitation studies revealed that OGFOD1 associates with a small subset of stress granule proteins (G3BP1, USP10, Caprin1, and YB-1) and the ribosome in both unstressed and stressed cells. Overexpression of OGFOD1 led to increased abundance of phosphorylated eIF2alpha, both in unstressed cells and in cells exposed to arsenite-induced stress, and to accelerated apoptosis during stress. Conversely, knockdown of OGFOD1 resulted in smaller amounts of phosphorylated eIF2alpha and a faster accumulation of polyribosomes in cells recovering from stress. Finally, OGFOD1 interacted with both eIF2alpha and the eIF2alpha kinase heme-regulated inhibitor (HRI), which was identified as a novel stress granule resident. These findings argue that OGFOD1 plays important proapoptotic roles in the regulation of translation and HRI-mediated phosphorylation of eIF2alpha in cells subjected to arsenite-induced stress.
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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/Arsenites,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/G3BP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Teratogens,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin,
http://linkedlifedata.com/resource/pubmed/chemical/USP10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin Thiolesterase,
http://linkedlifedata.com/resource/pubmed/chemical/arsenite
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1098-5549
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2006-16
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pubmed:dateRevised |
2010-10-4
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pubmed:meshHeading |
pubmed-meshheading:20154146-Animals,
pubmed-meshheading:20154146-Apoptosis,
pubmed-meshheading:20154146-Arsenites,
pubmed-meshheading:20154146-Carrier Proteins,
pubmed-meshheading:20154146-Enzyme Inhibitors,
pubmed-meshheading:20154146-Eukaryotic Initiation Factor-2,
pubmed-meshheading:20154146-HeLa Cells,
pubmed-meshheading:20154146-Humans,
pubmed-meshheading:20154146-Nuclear Proteins,
pubmed-meshheading:20154146-Oxidative Stress,
pubmed-meshheading:20154146-Phosphorylation,
pubmed-meshheading:20154146-Protein Biosynthesis,
pubmed-meshheading:20154146-RNA, Small Interfering,
pubmed-meshheading:20154146-Teratogens,
pubmed-meshheading:20154146-Thapsigargin,
pubmed-meshheading:20154146-Ubiquitin Thiolesterase
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pubmed:year |
2010
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pubmed:articleTitle |
OGFOD1, a novel modulator of eukaryotic translation initiation factor 2alpha phosphorylation and the cellular response to stress.
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pubmed:affiliation |
Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USAA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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