Source:http://linkedlifedata.com/resource/pubmed/id/11123929
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
51
|
| pubmed:dateCreated |
2001-1-8
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| pubmed:abstractText |
Regulation of eIF2alpha phosphorylation is critical to the maintenance of cellular homeostasis, and eIF2alpha kinases are subject to complex and multidimensional controls. A cellular 67 kDa glycoprotein (p67) has been proposed to have an important role in regulating the activity of eIF2alpha kinases including the interferon-induced, dsRNA-stimulated protein kinase PKR. To dissect p67-PKR interactions and evaluate their significance in vivo, we have used a vaccinia virus (VV) expression system that successfully mimics PKR control pathways. Recombinant VV were constructed that constitutively express p67 and inducibly express PKR in BSC-40 cells. Stable expression of p67 reduced the PKR-mediated antiviral response and apoptosis. These effects correlated with decreased eIF2alpha phosphorylation, with rescue of PKR-mediated inhibition of protein synthesis, and with partial inhibition of PKR-triggered activation of NF-kappaB. The direct interaction between PKR and p67 was suggested by in vivo and in vitro analyses. These data demonstrate that in vivo p67 is an important modulator of PKR-mediated signal transduction pathways and may provide a useful tool to dissect the relative contributions of PKR to cell growth and stress response.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/METAP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-2 Kinase
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
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| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
26
|
| pubmed:volume |
39
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
16016-25
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:11123929-Aminopeptidases,
pubmed-meshheading:11123929-Animals,
pubmed-meshheading:11123929-Antiviral Agents,
pubmed-meshheading:11123929-Apoptosis,
pubmed-meshheading:11123929-Cell Line,
pubmed-meshheading:11123929-Gene Expression Regulation, Viral,
pubmed-meshheading:11123929-Glycoproteins,
pubmed-meshheading:11123929-Humans,
pubmed-meshheading:11123929-NF-kappa B,
pubmed-meshheading:11123929-Phosphorylation,
pubmed-meshheading:11123929-Protein Binding,
pubmed-meshheading:11123929-Protein Biosynthesis,
pubmed-meshheading:11123929-RNA, Double-Stranded,
pubmed-meshheading:11123929-Recombination, Genetic,
pubmed-meshheading:11123929-Transcriptional Activation,
pubmed-meshheading:11123929-Up-Regulation,
pubmed-meshheading:11123929-Vaccinia virus,
pubmed-meshheading:11123929-Viral Proteins,
pubmed-meshheading:11123929-eIF-2 Kinase
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| pubmed:year |
2000
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| pubmed:articleTitle |
In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67.
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| pubmed:affiliation |
Department of Molecular and Cellular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus Universidad Autónoma, 28049 Madrid, Spain.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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