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The 40 S -LARP1 complex reprograms the cellular translatome upon mTOR inhibition to preserve the protein synthetic capacity 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 Ribosomes Síntesi proteica Ribosomes Protein synthesis 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. 2021-12-09T13:28:36Z 2021-12-09T13:28:36Z 2021-11-26 2021-12-02T08:46:46Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 cc by-nc (c) Fuentes, Pedro et al, 2021 http://creativecommons.org/licenses/by-nc/3.0/es/ info:eu-repo/semantics/openAccess American Association for the Advancement of Science (AAAS) Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))