Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN

Increasing evidence points to the Survival Motor Neuron (SMN) protein as a key determinant of translation pathway. Besides its role in RNA processing and sorting, several works support a critical implication of SMN in ribosome biogenesis. We previously showed that SMN binds ribosomal proteins (RPs)...

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Autores principales:	Francesca Gabanella, Christian Barbato, Marco Fiore, Carla Petrella, Marco de Vincentiis, Antonio Greco, Antonio Minni, Nicoletta Corbi, Claudio Passananti, Maria Grazia Di Certo
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	SMN nucleolin nucleolus ribosome biogenesis mTOR RNA translation Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3f3840099b40440d9a1fd6e0a884ea45
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spelling	oai:doaj.org-article:3f3840099b40440d9a1fd6e0a884ea452021-11-25T17:10:26ZFine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN10.3390/cells101130152073-4409https://doaj.org/article/3f3840099b40440d9a1fd6e0a884ea452021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4409/10/11/3015https://doaj.org/toc/2073-4409Increasing evidence points to the Survival Motor Neuron (SMN) protein as a key determinant of translation pathway. Besides its role in RNA processing and sorting, several works support a critical implication of SMN in ribosome biogenesis. We previously showed that SMN binds ribosomal proteins (RPs) as well as their encoding transcripts, ensuring an appropriate level of locally synthesized RPs. SMN impacts the translation machinery in both neural and non-neural cells, in agreement with the concept that SMN is an essential protein in all cell types. Here, we further assessed the relationship between SMN and translation-related factors in immortalized human fibroblasts. We focused on SMN-nucleolin interaction, keeping in mind that nucleolin is an RNA-binding protein, highly abundant within the nucleolus, that exhibits a central role in ribosomes production. Nucleolin may also affects translation network by binding the mammalian target of rapamycin (mTOR) mRNA and promoting its local synthesis. In this regard, for the first time we provided evidence that SMN protein itself associates with mTOR transcript. Collectively, we found that: (1) SMN coexists with nucleolin–mTOR mRNA complexes at subcellular level; (2) SMN deficiency impairs nucleolar compartmentalization of nucleolin, and (3) this event correlates with the nuclear retention of mTOR mRNA. These findings suggest that SMN may regulate not only structural components of translation machinery, but also their upstream regulating factors.Francesca GabanellaChristian BarbatoMarco FioreCarla PetrellaMarco de VincentiisAntonio GrecoAntonio MinniNicoletta CorbiClaudio PassanantiMaria Grazia Di CertoMDPI AGarticleSMNnucleolinnucleolusribosome biogenesismTORRNA translationBiology (General)QH301-705.5ENCells, Vol 10, Iss 3015, p 3015 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	SMN nucleolin nucleolus ribosome biogenesis mTOR RNA translation Biology (General) QH301-705.5
spellingShingle	SMN nucleolin nucleolus ribosome biogenesis mTOR RNA translation Biology (General) QH301-705.5 Francesca Gabanella Christian Barbato Marco Fiore Carla Petrella Marco de Vincentiis Antonio Greco Antonio Minni Nicoletta Corbi Claudio Passananti Maria Grazia Di Certo Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
description	Increasing evidence points to the Survival Motor Neuron (SMN) protein as a key determinant of translation pathway. Besides its role in RNA processing and sorting, several works support a critical implication of SMN in ribosome biogenesis. We previously showed that SMN binds ribosomal proteins (RPs) as well as their encoding transcripts, ensuring an appropriate level of locally synthesized RPs. SMN impacts the translation machinery in both neural and non-neural cells, in agreement with the concept that SMN is an essential protein in all cell types. Here, we further assessed the relationship between SMN and translation-related factors in immortalized human fibroblasts. We focused on SMN-nucleolin interaction, keeping in mind that nucleolin is an RNA-binding protein, highly abundant within the nucleolus, that exhibits a central role in ribosomes production. Nucleolin may also affects translation network by binding the mammalian target of rapamycin (mTOR) mRNA and promoting its local synthesis. In this regard, for the first time we provided evidence that SMN protein itself associates with mTOR transcript. Collectively, we found that: (1) SMN coexists with nucleolin–mTOR mRNA complexes at subcellular level; (2) SMN deficiency impairs nucleolar compartmentalization of nucleolin, and (3) this event correlates with the nuclear retention of mTOR mRNA. These findings suggest that SMN may regulate not only structural components of translation machinery, but also their upstream regulating factors.
format	article
author	Francesca Gabanella Christian Barbato Marco Fiore Carla Petrella Marco de Vincentiis Antonio Greco Antonio Minni Nicoletta Corbi Claudio Passananti Maria Grazia Di Certo
author_facet	Francesca Gabanella Christian Barbato Marco Fiore Carla Petrella Marco de Vincentiis Antonio Greco Antonio Minni Nicoletta Corbi Claudio Passananti Maria Grazia Di Certo
author_sort	Francesca Gabanella
title	Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
title_short	Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
title_full	Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
title_fullStr	Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
title_full_unstemmed	Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN
title_sort	fine-tuning of mtor mrna and nucleolin complexes by smn
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/3f3840099b40440d9a1fd6e0a884ea45
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Fine-Tuning of mTOR mRNA and Nucleolin Complexes by SMN

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