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Activation of GCN2 upon HIV-1 infection and inhibition of translation.
| dc.rights.license | open | en_US |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | COSNEFROY, Ophélie | |
| dc.contributor.author | JASPART, Anaïs | |
| dc.contributor.author | CALMELS, Christina | |
| dc.contributor.author | PARISSI, Vincent | |
| dc.contributor.author | FLEURY, Hervé | |
| dc.contributor.author | VENTURA, Michel | |
| dc.contributor.author | REIGADAS, Sandrine | |
| dc.contributor.author | ANDRÉOLA, Marie-Line | |
| dc.date.accessioned | 2024-11-15T13:42:16Z | |
| dc.date.available | 2024-11-15T13:42:16Z | |
| dc.date.issued | 2013-07-01 | |
| dc.identifier.issn | 1420-9071 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/203313 | |
| dc.description.abstractEn | Higher eukaryotic organisms have a variety of specific and nonspecific defense mechanisms against viral invaders. In animal cells, viral replication may be limited through the decrease in translation. Some viruses, however, have evolved mechanisms that counteract the response of the host. We report that infection by HIV-1 triggers acute decrease in translation. The human protein kinase GCN2 (eIF2AK4) is activated by phosphorylation upon HIV-1 infection in the hours following infection. Thus, infection by HIV-1 constitutes a stress that leads to the activation of GCN2 with a resulting decrease in protein synthesis. We have shown that GCN2 interacts with HIV-1 integrase (IN). Transfection of IN in amino acid-starved cells, where GCN2 is activated, increases the protein synthesis level. These results point to an as yet unknown role of GCN2 as an early mediator in the cellular response to HIV-1 infection, and suggest that the virus is able to overcome the involvement of GCN2 in the cellular response by eliciting methods to maintain protein synthesis. | |
| dc.language.iso | EN | en_US |
| dc.subject.en | Gene Silencing | |
| dc.subject.en | HIV Infections | |
| dc.subject.en | HIV Integrase | |
| dc.subject.en | HIV-1 | |
| dc.subject.en | HeLa Cells | |
| dc.subject.en | Humans | |
| dc.subject.en | Phosphorylation | |
| dc.subject.en | Protein Biosynthesis | |
| dc.subject.en | Protein Serine-Threonine Kinases | |
| dc.subject.en | Stress | |
| dc.subject.en | Physiological | |
| dc.subject.en | Virus Replication | |
| dc.title.en | Activation of GCN2 upon HIV-1 infection and inhibition of translation. | |
| dc.title.alternative | Cell Mol Life Sci | en_US |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1007/s00018-013-1272-x | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Médecine humaine et pathologie | en_US |
| dc.identifier.pubmed | 23417324 | en_US |
| bordeaux.journal | Cellular and Molecular Life Sciences | en_US |
| bordeaux.page | 2411-21 | en_US |
| bordeaux.volume | 70 | en_US |
| bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
| bordeaux.issue | 13 | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| bordeaux.import.source | pubmed | |
| hal.popular | non | en_US |
| hal.audience | Internationale | en_US |
| hal.export | false | |
| workflow.import.source | pubmed | |
| dc.rights.cc | Pas de Licence CC | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Cellular%20and%20Molecular%20Life%20Sciences&rft.date=2013-07-01&rft.volume=70&rft.issue=13&rft.spage=2411-21&rft.epage=2411-21&rft.eissn=1420-9071&rft.issn=1420-9071&rft.au=COSNEFROY,%20Oph%C3%A9lie&JASPART,%20Ana%C3%AFs&CALMELS,%20Christina&PARISSI,%20Vincent&FLEURY,%20Herv%C3%A9&rft.genre=article |
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