The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity

Ribosomes execute the transcriptional program in every cell. Critical to sustain nearly all cellular activities, ribosome biogenesis requires the translation of ~200 factors of which 80 are ribosomal proteins (RPs). As ribosome synthesis depends on RP mRNA translation, a priority within the translat...

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Autores: Fuentes, Pedro, Pelletier, Joffrey, Martinez Herráez, Carolina, Diez Obrero, Virginia, Iannizzotto, Flavia, Rubio, Teresa, Garcia Cajide, Marta, Menoyo, Sandra, Moreno Aguado, Víctor, Salazar, Ramón, Tauler Girona, Albert, Gentilella, Antonio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/181680
Acceso en línea:https://hdl.handle.net/2445/181680
Access Level:acceso abierto
Palabra clave:Ribosomes
Síntesi proteica
Protein synthesis
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spelling The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacityFuentes, PedroPelletier, JoffreyMartinez Herráez, CarolinaDiez Obrero, VirginiaIannizzotto, FlaviaRubio, TeresaGarcia Cajide, MartaMenoyo, SandraMoreno Aguado, VíctorSalazar, RamónTauler Girona, AlbertGentilella, AntonioRibosomesSíntesi proteicaRibosomesProtein synthesisRibosomes execute the transcriptional program in every cell. Critical to sustain nearly all cellular activities, ribosome biogenesis requires the translation of ~200 factors of which 80 are ribosomal proteins (RPs). As ribosome synthesis depends on RP mRNA translation, a priority within the translatome architecture should exist to ensure the preservation of ribosome biogenesis capacity, particularly under adverse growth conditions. Here, we show that under critical metabolic constraints characterized by mTOR inhibition, LARP1 complexed with the 40S subunit protects from ribophagy the mRNAs regulon for ribosome biogenesis and protein synthesis, acutely preparing the translatome to promptly resume ribosomes production after growth conditions return permissive. Characterizing the LARP1-protected translatome revealed a set of 5′TOP transcript isoforms other than RPs involved in energy production and in mitochondrial function, among other processes, indicating that the mTOR-LARP1-5′TOP axis acts at the translational level as a primary guardian of the cellular anabolic capacity.American Association for the Advancement of Science (AAAS)2021202120212021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion16 p.application/pdfapplication/pdfhttps://hdl.handle.net/2445/181680Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1126/sciadv.abg9275Science Advances, 2021, vol. 7, num. 48https://doi.org/10.1126/sciadv.abg9275cc by-nc (c) Fuentes, Pedro et al, 2021http://creativecommons.org/licenses/by-nc/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1816802026-05-29T05:05:01Z
dc.title.none.fl_str_mv The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
title The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
spellingShingle The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
Fuentes, Pedro
Ribosomes
Síntesi proteica
Ribosomes
Protein synthesis
title_short The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
title_full The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
title_fullStr The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
title_full_unstemmed The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
title_sort The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity
dc.creator.none.fl_str_mv Fuentes, Pedro
Pelletier, Joffrey
Martinez Herráez, Carolina
Diez Obrero, Virginia
Iannizzotto, Flavia
Rubio, Teresa
Garcia Cajide, Marta
Menoyo, Sandra
Moreno Aguado, Víctor
Salazar, Ramón
Tauler Girona, Albert
Gentilella, Antonio
author Fuentes, Pedro
author_facet Fuentes, Pedro
Pelletier, Joffrey
Martinez Herráez, Carolina
Diez Obrero, Virginia
Iannizzotto, Flavia
Rubio, Teresa
Garcia Cajide, Marta
Menoyo, Sandra
Moreno Aguado, Víctor
Salazar, Ramón
Tauler Girona, Albert
Gentilella, Antonio
author_role author
author2 Pelletier, Joffrey
Martinez Herráez, Carolina
Diez Obrero, Virginia
Iannizzotto, Flavia
Rubio, Teresa
Garcia Cajide, Marta
Menoyo, Sandra
Moreno Aguado, Víctor
Salazar, Ramón
Tauler Girona, Albert
Gentilella, Antonio
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ribosomes
Síntesi proteica
Ribosomes
Protein synthesis
topic Ribosomes
Síntesi proteica
Ribosomes
Protein synthesis
description Ribosomes execute the transcriptional program in every cell. Critical to sustain nearly all cellular activities, ribosome biogenesis requires the translation of ~200 factors of which 80 are ribosomal proteins (RPs). As ribosome synthesis depends on RP mRNA translation, a priority within the translatome architecture should exist to ensure the preservation of ribosome biogenesis capacity, particularly under adverse growth conditions. Here, we show that under critical metabolic constraints characterized by mTOR inhibition, LARP1 complexed with the 40S subunit protects from ribophagy the mRNAs regulon for ribosome biogenesis and protein synthesis, acutely preparing the translatome to promptly resume ribosomes production after growth conditions return permissive. Characterizing the LARP1-protected translatome revealed a set of 5′TOP transcript isoforms other than RPs involved in energy production and in mitochondrial function, among other processes, indicating that the mTOR-LARP1-5′TOP axis acts at the translational level as a primary guardian of the cellular anabolic capacity.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/181680
url https://hdl.handle.net/2445/181680
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1126/sciadv.abg9275
Science Advances, 2021, vol. 7, num. 48
https://doi.org/10.1126/sciadv.abg9275
dc.rights.none.fl_str_mv cc by-nc (c) Fuentes, Pedro et al, 2021
http://creativecommons.org/licenses/by-nc/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by-nc (c) Fuentes, Pedro et al, 2021
http://creativecommons.org/licenses/by-nc/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 16 p.
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Association for the Advancement of Science (AAAS)
publisher.none.fl_str_mv American Association for the Advancement of Science (AAAS)
dc.source.none.fl_str_mv Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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