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The translational factor eIF3f: the ambivalent eIF3 subunit

The regulation of the protein synthesis has a crucial role in governing the eukaryotic cell growth. Subtle changes of proteins involved in the translation process may alter the rate of the protein synthesis and modify the cell fate by shifting the balance from normal status into a tumoral or apoptot...

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Detalles Bibliográficos
Autores principales: Marchione, Roberta, Leibovitch, Serge A., Lenormand, Jean-Luc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Basel 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771369/
https://www.ncbi.nlm.nih.gov/pubmed/23354061
http://dx.doi.org/10.1007/s00018-013-1263-y
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author Marchione, Roberta
Leibovitch, Serge A.
Lenormand, Jean-Luc
author_facet Marchione, Roberta
Leibovitch, Serge A.
Lenormand, Jean-Luc
author_sort Marchione, Roberta
collection PubMed
description The regulation of the protein synthesis has a crucial role in governing the eukaryotic cell growth. Subtle changes of proteins involved in the translation process may alter the rate of the protein synthesis and modify the cell fate by shifting the balance from normal status into a tumoral or apoptotic one. The largest eukaryotic initiation factor involved in translation regulation is eIF3. Amongst the 13 factors constituting eIF3, the f subunit finely regulates this balance in a cell-type-specific manner. Loss of this factor causes malignancy in several cells, and atrophy in normal muscle cells. The intracellular interacting partners which influence its physiological significance in both cancer and muscle cells are detailed in this review. By delineating the global interaction network of this factor and by clarifying its intracellular role, it becomes apparent that the f subunit represents a promising candidate molecule to use for biotherapeutic applications.
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spelling pubmed-37713692013-09-13 The translational factor eIF3f: the ambivalent eIF3 subunit Marchione, Roberta Leibovitch, Serge A. Lenormand, Jean-Luc Cell Mol Life Sci Review The regulation of the protein synthesis has a crucial role in governing the eukaryotic cell growth. Subtle changes of proteins involved in the translation process may alter the rate of the protein synthesis and modify the cell fate by shifting the balance from normal status into a tumoral or apoptotic one. The largest eukaryotic initiation factor involved in translation regulation is eIF3. Amongst the 13 factors constituting eIF3, the f subunit finely regulates this balance in a cell-type-specific manner. Loss of this factor causes malignancy in several cells, and atrophy in normal muscle cells. The intracellular interacting partners which influence its physiological significance in both cancer and muscle cells are detailed in this review. By delineating the global interaction network of this factor and by clarifying its intracellular role, it becomes apparent that the f subunit represents a promising candidate molecule to use for biotherapeutic applications. Springer Basel 2013-01-25 2013 /pmc/articles/PMC3771369/ /pubmed/23354061 http://dx.doi.org/10.1007/s00018-013-1263-y Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Review
Marchione, Roberta
Leibovitch, Serge A.
Lenormand, Jean-Luc
The translational factor eIF3f: the ambivalent eIF3 subunit
title The translational factor eIF3f: the ambivalent eIF3 subunit
title_full The translational factor eIF3f: the ambivalent eIF3 subunit
title_fullStr The translational factor eIF3f: the ambivalent eIF3 subunit
title_full_unstemmed The translational factor eIF3f: the ambivalent eIF3 subunit
title_short The translational factor eIF3f: the ambivalent eIF3 subunit
title_sort translational factor eif3f: the ambivalent eif3 subunit
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771369/
https://www.ncbi.nlm.nih.gov/pubmed/23354061
http://dx.doi.org/10.1007/s00018-013-1263-y
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