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Type: Journal article
Title: Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
Author: Mendes, A.
Gigan, J.P.
Rodriguez Rodrigues, C.
Choteau, S.A.
Sanseau, D.
Barros, D.
Almeida, C.
Camosseto, V.
Chasson, L.
Paton, A.W.
Paton, J.C.
Argüello, R.J.
Lennon-Duménil, A.-M.
Gatti, E.
Pierre, P.
Citation: Life Science Alliance, 2021; 4(2):1-22
Publisher: Life Science Alliance
Issue Date: 2021
ISSN: 2575-1077
Statement of
Andreia Mendes, Julien P Gigan, Christian Rodriguez Rodrigues, Sébastien A Choteau, Doriane Sanseau, Daniela Barros ... et al.
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.
Keywords: Spleen
Dendritic Cells
eIF-2 Kinase
Membrane Proteins
Signal Transduction
Cell Movement
Activating Transcription Factor 4
Protein Multimerization
Gene Knockdown Techniques
Rights: © 2020 Mendes et al. This article is available under a Creative Commons License (Attribution 4.0 International, as described at licenses/by/4.0/).
DOI: 10.26508/lsa.202000865
Appears in Collections:Aurora harvest 4
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