Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4

Autores
Mendes, Andreia; Gigan, Julien P.; Rodríguez Rodrígues, Christian Fernando Ariel; Choteau, Sébastien A.; Sanseau, Doriane; Barros, Daniela; Almeida, Catarina; Camosseto, Voahirana; Chasson, Lionel; Paton, Adrienne W.; Paton, James C.; Argüello, Rafael José; Lennon Duménil, Ana Maria; Gatti, Evelina; Pierre, Philippe
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Mendes, Andreia. Inserm; Francia
Fil: Gigan, Julien P.. Inserm; Francia
Fil: Rodríguez Rodrígues, Christian Fernando Ariel. Universidad Nacional de Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente; Argentina
Fil: Choteau, Sébastien A.. Inserm; Francia
Fil: Sanseau, Doriane. Inserm; Francia
Fil: Barros, Daniela. Inserm; Francia
Fil: Almeida, Catarina. Centre National de la Recherche Scientifique; Francia
Fil: Camosseto, Voahirana. Inserm; Francia
Fil: Chasson, Lionel. Inserm; Francia
Fil: Paton, Adrienne W.. University of Adelaide; Australia
Fil: Paton, James C.. University of Adelaide; Australia
Fil: Argüello, Rafael José. Inserm; Francia
Fil: Lennon Duménil, Ana Maria. Inserm; Francia
Fil: Gatti, Evelina. Inserm; Francia
Fil: Pierre, Philippe. Inserm; Francia
Materia
PROTEOSTASIS
PERK
DENDRITIC CELL
EIF2A
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/155042
Acceder
id CONICETDig_7cd15a0a5d4ea12dff59587fdf93f9a6
oai_identifier_str oai:ri.conicet.gov.ar:11336/155042
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4Mendes, AndreiaGigan, Julien P.Rodríguez Rodrígues, Christian Fernando ArielChoteau, Sébastien A.Sanseau, DorianeBarros, DanielaAlmeida, CatarinaCamosseto, VoahiranaChasson, LionelPaton, Adrienne W.Paton, James C.Argüello, Rafael JoséLennon Duménil, Ana MariaGatti, EvelinaPierre, PhilippePROTEOSTASISPERKDENDRITIC CELLEIF2Ahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In 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.Fil: Mendes, Andreia. Inserm; FranciaFil: Gigan, Julien P.. Inserm; FranciaFil: Rodríguez Rodrígues, Christian Fernando Ariel. Universidad Nacional de Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente; ArgentinaFil: Choteau, Sébastien A.. Inserm; FranciaFil: Sanseau, Doriane. Inserm; FranciaFil: Barros, Daniela. Inserm; FranciaFil: Almeida, Catarina. Centre National de la Recherche Scientifique; FranciaFil: Camosseto, Voahirana. Inserm; FranciaFil: Chasson, Lionel. Inserm; FranciaFil: Paton, Adrienne W.. University of Adelaide; AustraliaFil: Paton, James C.. University of Adelaide; AustraliaFil: Argüello, Rafael José. Inserm; FranciaFil: Lennon Duménil, Ana Maria. Inserm; FranciaFil: Gatti, Evelina. Inserm; FranciaFil: Pierre, Philippe. Inserm; FranciaRockefeller University Press2021-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/155042Mendes, Andreia; Gigan, Julien P.; Rodríguez Rodrígues, Christian Fernando Ariel; Choteau, Sébastien A.; Sanseau, Doriane; et al.; Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4; Rockefeller University Press; Life Science Alliance; 4; 2; 2-2021; 1-222575-1077CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.life-science-alliance.org/content/4/2/e202000865.abstractinfo:eu-repo/semantics/altIdentifier/doi/10.26508/lsa.202000865info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:24:43Zoai:ri.conicet.gov.ar:11336/155042instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:24:43.421CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
title Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
spellingShingle Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
Mendes, Andreia
PROTEOSTASIS
PERK
DENDRITIC CELL
EIF2A
title_short Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
title_full Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
title_fullStr Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
title_full_unstemmed Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
title_sort Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4
dc.creator.none.fl_str_mv Mendes, Andreia
Gigan, Julien P.
Rodríguez Rodrígues, Christian Fernando Ariel
Choteau, Sébastien A.
Sanseau, Doriane
Barros, Daniela
Almeida, Catarina
Camosseto, Voahirana
Chasson, Lionel
Paton, Adrienne W.
Paton, James C.
Argüello, Rafael José
Lennon Duménil, Ana Maria
Gatti, Evelina
Pierre, Philippe
author Mendes, Andreia
author_facet Mendes, Andreia
Gigan, Julien P.
Rodríguez Rodrígues, Christian Fernando Ariel
Choteau, Sébastien A.
Sanseau, Doriane
Barros, Daniela
Almeida, Catarina
Camosseto, Voahirana
Chasson, Lionel
Paton, Adrienne W.
Paton, James C.
Argüello, Rafael José
Lennon Duménil, Ana Maria
Gatti, Evelina
Pierre, Philippe
author_role author
author2 Gigan, Julien P.
Rodríguez Rodrígues, Christian Fernando Ariel
Choteau, Sébastien A.
Sanseau, Doriane
Barros, Daniela
Almeida, Catarina
Camosseto, Voahirana
Chasson, Lionel
Paton, Adrienne W.
Paton, James C.
Argüello, Rafael José
Lennon Duménil, Ana Maria
Gatti, Evelina
Pierre, Philippe
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv PROTEOSTASIS
PERK
DENDRITIC CELL
EIF2A
topic PROTEOSTASIS
PERK
DENDRITIC CELL
EIF2A
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Mendes, Andreia. Inserm; Francia
Fil: Gigan, Julien P.. Inserm; Francia
Fil: Rodríguez Rodrígues, Christian Fernando Ariel. Universidad Nacional de Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones en Producción, Sanidad y Ambiente; Argentina
Fil: Choteau, Sébastien A.. Inserm; Francia
Fil: Sanseau, Doriane. Inserm; Francia
Fil: Barros, Daniela. Inserm; Francia
Fil: Almeida, Catarina. Centre National de la Recherche Scientifique; Francia
Fil: Camosseto, Voahirana. Inserm; Francia
Fil: Chasson, Lionel. Inserm; Francia
Fil: Paton, Adrienne W.. University of Adelaide; Australia
Fil: Paton, James C.. University of Adelaide; Australia
Fil: Argüello, Rafael José. Inserm; Francia
Fil: Lennon Duménil, Ana Maria. Inserm; Francia
Fil: Gatti, Evelina. Inserm; Francia
Fil: Pierre, Philippe. Inserm; Francia
description 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.
publishDate 2021
dc.date.none.fl_str_mv 2021-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/155042
Mendes, Andreia; Gigan, Julien P.; Rodríguez Rodrígues, Christian Fernando Ariel; Choteau, Sébastien A.; Sanseau, Doriane; et al.; Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4; Rockefeller University Press; Life Science Alliance; 4; 2; 2-2021; 1-22
2575-1077
CONICET Digital
CONICET
url http://hdl.handle.net/11336/155042
identifier_str_mv Mendes, Andreia; Gigan, Julien P.; Rodríguez Rodrígues, Christian Fernando Ariel; Choteau, Sébastien A.; Sanseau, Doriane; et al.; Proteostasis in dendritic cells is controlled by the PERK signaling axis independently of ATF4; Rockefeller University Press; Life Science Alliance; 4; 2; 2-2021; 1-22
2575-1077
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.life-science-alliance.org/content/4/2/e202000865.abstract
info:eu-repo/semantics/altIdentifier/doi/10.26508/lsa.202000865
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Rockefeller University Press
publisher.none.fl_str_mv Rockefeller University Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781788801728512
score 12.982451

Publicaciones similares