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...
| Autores: | , , , , , , , , , , , |
|---|---|
| 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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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 |
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| repository.mail.fl_str_mv |
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15,812429 |