Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/130640
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dc.contributor.author | Mendes, A. | - |
dc.contributor.author | Gigan, J.P. | - |
dc.contributor.author | Rodriguez Rodrigues, C. | - |
dc.contributor.author | Choteau, S.A. | - |
dc.contributor.author | Sanseau, D. | - |
dc.contributor.author | Barros, D. | - |
dc.contributor.author | Almeida, C. | - |
dc.contributor.author | Camosseto, V. | - |
dc.contributor.author | Chasson, L. | - |
dc.contributor.author | Paton, A.W. | - |
dc.contributor.author | Paton, J.C. | - |
dc.contributor.author | Argüello, R.J. | - |
dc.contributor.author | Lennon-Duménil, A.-M. | - |
dc.contributor.author | Gatti, E. | - |
dc.contributor.author | Pierre, P. | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | Life Science Alliance, 2021; 4(2):1-22 | - |
dc.identifier.issn | 2575-1077 | - |
dc.identifier.issn | 2575-1077 | - |
dc.identifier.uri | http://hdl.handle.net/2440/130640 | - |
dc.description.abstract | In stressed cells, phosphorylation of eukaryotic initiation factor 2α (eIF2α) controls transcriptome-wide changes in mRNA translation and gene expression known as the integrated stress response. We show here that DCs are characterized by high eIF2α phosphorylation, mostly caused by the activation of the ER kinase PERK (EIF2AK3). Despite high p-eIF2α levels, DCs display active protein synthesis and no signs of a chronic integrated stress response. This biochemical specificity prevents translation arrest and expression of the transcription factor ATF4 during ER-stress induction by the subtilase cytotoxin (SubAB). PERK inactivation, increases globally protein synthesis levels and regulates IFN-β expression, while impairing LPS-stimulated DC migration. Although the loss of PERK activity does not impact DC development, the cross talk existing between actin cytoskeleton dynamics; PERK and eIF2α phosphorylation is likely important to adapt DC homeostasis to the variations imposed by the immune contexts. | - |
dc.description.statementofresponsibility | Andreia Mendes, Julien P Gigan, Christian Rodriguez Rodrigues, Sébastien A Choteau, Doriane Sanseau, Daniela Barros ... et al. | - |
dc.language.iso | en | - |
dc.publisher | Life Science Alliance | - |
dc.rights | © 2020 Mendes et al. This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/ licenses/by/4.0/). | - |
dc.source.uri | http://dx.doi.org/10.26508/lsa.202000865 | - |
dc.subject | Spleen | - |
dc.subject | Dendritic Cells | - |
dc.subject | Animals | - |
dc.subject | Mice | - |
dc.subject | Actins | - |
dc.subject | Subtilisins | - |
dc.subject | eIF-2 Kinase | - |
dc.subject | Lipopolysaccharides | - |
dc.subject | Membrane Proteins | - |
dc.subject | Antigens | - |
dc.subject | Cytokines | - |
dc.subject | Signal Transduction | - |
dc.subject | Cell Movement | - |
dc.subject | Phosphorylation | - |
dc.subject | Activating Transcription Factor 4 | - |
dc.subject | Protein Multimerization | - |
dc.subject | Gene Knockdown Techniques | - |
dc.subject | Proteostasis | - |
dc.title | Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4 | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.26508/lsa.202000865 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Paton, J.C. [0000-0001-9807-5278] | - |
Appears in Collections: | Aurora harvest 4 Medicine publications |
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hdl_130640.pdf | 4.29 MB | Adobe PDF | View/Open |
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