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rdf:type |
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lifeskim:mentions |
umls-concept:C0040649,
umls-concept:C0040711,
umls-concept:C0073337,
umls-concept:C0243077,
umls-concept:C1136224,
umls-concept:C1138405,
umls-concept:C1307407,
umls-concept:C1414805,
umls-concept:C1704259,
umls-concept:C1705621,
umls-concept:C1705987,
umls-concept:C1710082,
umls-concept:C1879547
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pubmed:issue |
22
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pubmed:dateCreated |
2000-12-5
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pubmed:abstractText |
We have analysed the effect of transcription inhibitors on the polysomal localization of 5' terminal oligopyrimidine (TOP-) mRNAs. It is known that, in vertebrates, the translation of this group of mRNAs is regulated according to the growth status of the cell. Mitogenic stimulation of quiescent cells induces a rapid recruitment of TOP mRNAs from translationally inactive light messenger ribonucleoprotein particles to polysomes. It was found that administration of transcription inhibitors to resting cells causes a similar collective translational activation of TOP mRNAs, without affecting global translation. A number of transcription inhibitors were tested in amphibian and mammalian cultured cells. Actinomycin D (act D), cordycepin, and 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole caused a similar activation whereas alpha-amanitin or low doses of act D did not induce the translational response. Concentrations of act D sufficient to induce TOP mRNA translation also induce 40S ribosomal protein S6 kinases 1 (S6K1) activation. Moreover at these concentrations of act D increased phosphorylation of 4E-BP1 was also observed, indicating the involvement of FRAP/mTOR. Consistent with this observation, pretreatment of resting cells with rapamycin suppresses the activation of TOP mRNA translation induced by act D. These results indicate that the effect of act D on translation is mediated by the S6Ks through FRAP/mTOR.
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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/Amanitins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dactinomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyadenosines,
http://linkedlifedata.com/resource/pubmed/chemical/Dichlororibofuranosylbenzimidazole,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acid Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Protein S6 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cordycepin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6594-601
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11054111-Amanitins,
pubmed-meshheading:11054111-Animals,
pubmed-meshheading:11054111-Cell Cycle Proteins,
pubmed-meshheading:11054111-Cells, Cultured,
pubmed-meshheading:11054111-Dactinomycin,
pubmed-meshheading:11054111-Deoxyadenosines,
pubmed-meshheading:11054111-Dichlororibofuranosylbenzimidazole,
pubmed-meshheading:11054111-Enzyme Activation,
pubmed-meshheading:11054111-Kidney,
pubmed-meshheading:11054111-Nucleic Acid Synthesis Inhibitors,
pubmed-meshheading:11054111-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:11054111-Protein Biosynthesis,
pubmed-meshheading:11054111-Protein Kinases,
pubmed-meshheading:11054111-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11054111-RNA, Messenger,
pubmed-meshheading:11054111-Ribosomal Protein S6 Kinases,
pubmed-meshheading:11054111-Signal Transduction,
pubmed-meshheading:11054111-TOR Serine-Threonine Kinases,
pubmed-meshheading:11054111-Transcription, Genetic,
pubmed-meshheading:11054111-Vertebrates,
pubmed-meshheading:11054111-Xenopus Proteins,
pubmed-meshheading:11054111-Xenopus laevis
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pubmed:year |
2000
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pubmed:articleTitle |
Transcription inhibitors stimulate translation of 5' TOP mRNAs through activation of S6 kinase and the mTOR/FRAP signalling pathway.
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pubmed:affiliation |
Dipartimento di Biologia, Universita' 'Tor Vergata', Roma, Italy; Department of Growth Control, Friedrich Miescher Institut, Basel, Switzerland. loreni@uniroma2.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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